PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10098879-1 1999 In this study, we have further delineated the domains of the N-methyl-D-aspartate receptor NR1 subunit that contribute to the glycine co-agonist binding site. Glycine 126-133 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 91-94 10780999-1 2000 The potency of two novel glycine site antagonists, GV150,526A and GV196,771A, was assessed by their ability to inhibit the binding of [(3)H]-MDL105,519 to cell homogenates prepared from mammalian cells transfected with either NR1-1a, NR1-2a, NR1-1a/NR2A, NR1-1a/NR2B, NR1-1a/NR2C or NR1-1a/NR2D NMDA receptor clones. Glycine 25-32 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 226-229 10780999-1 2000 The potency of two novel glycine site antagonists, GV150,526A and GV196,771A, was assessed by their ability to inhibit the binding of [(3)H]-MDL105,519 to cell homogenates prepared from mammalian cells transfected with either NR1-1a, NR1-2a, NR1-1a/NR2A, NR1-1a/NR2B, NR1-1a/NR2C or NR1-1a/NR2D NMDA receptor clones. Glycine 25-32 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 234-237 10780999-1 2000 The potency of two novel glycine site antagonists, GV150,526A and GV196,771A, was assessed by their ability to inhibit the binding of [(3)H]-MDL105,519 to cell homogenates prepared from mammalian cells transfected with either NR1-1a, NR1-2a, NR1-1a/NR2A, NR1-1a/NR2B, NR1-1a/NR2C or NR1-1a/NR2D NMDA receptor clones. Glycine 25-32 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 234-237 10780999-1 2000 The potency of two novel glycine site antagonists, GV150,526A and GV196,771A, was assessed by their ability to inhibit the binding of [(3)H]-MDL105,519 to cell homogenates prepared from mammalian cells transfected with either NR1-1a, NR1-2a, NR1-1a/NR2A, NR1-1a/NR2B, NR1-1a/NR2C or NR1-1a/NR2D NMDA receptor clones. Glycine 25-32 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 234-237 10780999-1 2000 The potency of two novel glycine site antagonists, GV150,526A and GV196,771A, was assessed by their ability to inhibit the binding of [(3)H]-MDL105,519 to cell homogenates prepared from mammalian cells transfected with either NR1-1a, NR1-2a, NR1-1a/NR2A, NR1-1a/NR2B, NR1-1a/NR2C or NR1-1a/NR2D NMDA receptor clones. Glycine 25-32 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 234-237 10780999-1 2000 The potency of two novel glycine site antagonists, GV150,526A and GV196,771A, was assessed by their ability to inhibit the binding of [(3)H]-MDL105,519 to cell homogenates prepared from mammalian cells transfected with either NR1-1a, NR1-2a, NR1-1a/NR2A, NR1-1a/NR2B, NR1-1a/NR2C or NR1-1a/NR2D NMDA receptor clones. Glycine 25-32 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 234-237 10780999-7 2000 The K(i)s for a series of glycine site ligands with diverse chemical structures were also determined for the inhibition of [(3)H]-MDL105,519 binding to NR1-1a/NR2A receptors. Glycine 26-33 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 152-155 10780999-9 2000 It is suggested that glycine site antagonists may be divided into two classes based on their ability to distinguish between NR1 and NR1/NR2 receptors with respect to binding curve characteristics. Glycine 21-28 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 124-127 10780999-9 2000 It is suggested that glycine site antagonists may be divided into two classes based on their ability to distinguish between NR1 and NR1/NR2 receptors with respect to binding curve characteristics. Glycine 21-28 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 132-135 10581413-0 1999 A mutation in the glycine binding pocket of the N-methyl-D-aspartate receptor NR1 subunit alters agonist efficacy. Glycine 18-25 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 78-81 10581413-1 1999 Alanine 714 of the NMDA receptor NR1 subunit resides in the glycine binding pocket. Glycine 60-67 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 33-36 10098879-2 1999 Taking an iterative approach, we have constructed truncation mutants of the NR1 subunit, transiently expressed them in HEK-293 cells, and determined the binding of the glycine site antagonist [3H]L-689,560. Glycine 168-175 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 76-79 10208572-3 1999 Since [3H]L-689,560, [3H]CGP 39653 and [3H]ifenprodil label the glycine, glutamate and ifenprodil sites of the NMDA receptor complex, which are associated with NR1, NR1/NR2A and NR1/NR2B subunits respectively, our findings suggest that NR2B-containing receptors are selectively up-regulated in superior temporal cortex in schizophrenia. Glycine 64-71 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 160-163 10208572-3 1999 Since [3H]L-689,560, [3H]CGP 39653 and [3H]ifenprodil label the glycine, glutamate and ifenprodil sites of the NMDA receptor complex, which are associated with NR1, NR1/NR2A and NR1/NR2B subunits respectively, our findings suggest that NR2B-containing receptors are selectively up-regulated in superior temporal cortex in schizophrenia. Glycine 64-71 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 165-168 10208572-3 1999 Since [3H]L-689,560, [3H]CGP 39653 and [3H]ifenprodil label the glycine, glutamate and ifenprodil sites of the NMDA receptor complex, which are associated with NR1, NR1/NR2A and NR1/NR2B subunits respectively, our findings suggest that NR2B-containing receptors are selectively up-regulated in superior temporal cortex in schizophrenia. Glycine 64-71 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 165-168 8863813-0 1996 Activation of N-methyl-D-aspartate receptors by glycine: role of an aspartate residue in the M3-M4 loop of the NR1 subunit. Glycine 48-55 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 111-114 9375665-4 1997 Brief application of an NMDA/glycine solution to cells markedly increased intracellular calcium in cells transfected with NR1/NR2A, NR1/NR2B, or NR1/NR2A/NR2B as measured by fura-2 calcium imaging. Glycine 29-36 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 122-125 9375665-4 1997 Brief application of an NMDA/glycine solution to cells markedly increased intracellular calcium in cells transfected with NR1/NR2A, NR1/NR2B, or NR1/NR2A/NR2B as measured by fura-2 calcium imaging. Glycine 29-36 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 132-135 9375665-4 1997 Brief application of an NMDA/glycine solution to cells markedly increased intracellular calcium in cells transfected with NR1/NR2A, NR1/NR2B, or NR1/NR2A/NR2B as measured by fura-2 calcium imaging. Glycine 29-36 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 132-135 9871463-4 1998 Glycine shows different affinities at various NMDA receptor subtypes probably via to allosteric interactions between NMDA2 subunits and the glycine recognition site on the NMDAR1 subunit. Glycine 0-7 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 172-178 9871463-4 1998 Glycine shows different affinities at various NMDA receptor subtypes probably via to allosteric interactions between NMDA2 subunits and the glycine recognition site on the NMDAR1 subunit. Glycine 140-147 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 172-178 9481670-10 1998 Substitutions of glycine, serine, glutamine or aspartate for the N-site asparagine in the NR1-subunit enhanced the extent of block over intermediate potentials but left the voltage dependence of the block unchanged indicating that structural determinants of the block remained. Glycine 17-24 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 90-93 9115742-2 1997 The glycine binding site of these heteromeric receptor proteins is formed by regions of the NMDAR1 (NR1) subunit that display sequence similarity to bacterial amino acid binding proteins. Glycine 4-11 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 92-98 9115742-2 1997 The glycine binding site of these heteromeric receptor proteins is formed by regions of the NMDAR1 (NR1) subunit that display sequence similarity to bacterial amino acid binding proteins. Glycine 4-11 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 100-103 9115742-6 1997 Homology-based molecular modeling of the glutamate and glycine binding domains indicates that the NR2 and NR1 subunits use similar residues to ligate the agonists" alpha-aminocarboxylic acid groups, whereas differences in side chain interactions and size of aromatic residues determine ligand selectivity. Glycine 55-62 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 106-109 8967993-9 1996 At saturating concentrations of NMDA (1 mM), NR1-1a/2A heteromers also showed Ca- and glycine-independent desensitization, as seen in native hippocampal neurons. Glycine 86-93 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 45-48 8967993-10 1996 Ca(2+)- and glycine-independent desensitization was less pronounced in NR1-1a/2B heteromers and absent in NR1-1a/2C heteromers. Glycine 12-19 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 71-74 8863813-8 1996 Residue D732 in NR1 may be close to a glycine binding site on the NMDA receptor and may directly affect the properties of this site or be critical for coupling of glycine binding to channel activation. Glycine 38-45 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 16-19 8863813-8 1996 Residue D732 in NR1 may be close to a glycine binding site on the NMDA receptor and may directly affect the properties of this site or be critical for coupling of glycine binding to channel activation. Glycine 163-170 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 16-19 8863813-3 1996 Mutations at NR1(D732) also changed sensitivity to the glycine-site agonists D-serine and D-alanine, reducing the potencies and, in some cases, the efficacies of these compounds. Glycine 55-62 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 13-16 8863813-4 1996 Thus, D-serine was a full agonist at the glycine site of receptors containing NR1(D732N) and NR1(D732A), a partial agonist at receptors containing NR1(D732G), and a competitive antagonist at receptors containing NR1(D732). Glycine 41-48 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 78-81 8863813-4 1996 Thus, D-serine was a full agonist at the glycine site of receptors containing NR1(D732N) and NR1(D732A), a partial agonist at receptors containing NR1(D732G), and a competitive antagonist at receptors containing NR1(D732). Glycine 41-48 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 93-96 8863813-4 1996 Thus, D-serine was a full agonist at the glycine site of receptors containing NR1(D732N) and NR1(D732A), a partial agonist at receptors containing NR1(D732G), and a competitive antagonist at receptors containing NR1(D732). Glycine 41-48 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 93-96 8863813-4 1996 Thus, D-serine was a full agonist at the glycine site of receptors containing NR1(D732N) and NR1(D732A), a partial agonist at receptors containing NR1(D732G), and a competitive antagonist at receptors containing NR1(D732). Glycine 41-48 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 93-96 8863813-5 1996 Mutations at NR1(D732) had no effect or produced an increase in sensitivity to the glycine-site antagonists 6,7-dichloroquinoxaline-2,3-dione and 5,7-dichlorokynurenic acid. Glycine 83-90 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 13-16 8650214-0 1996 The glycine binding site of the N-methyl-D-aspartate receptor subunit NR1: identification of novel determinants of co-agonist potentiation in the extracellular M3-M4 loop region. Glycine 4-11 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 32-73 8650214-2 1996 Here, the contribution of the M3-M4 loop of the NR1 subunit to the binding of glutamate and the co-agonist glycine was investigated by site-directed mutagenesis. Glycine 107-114 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 48-51 8650214-6 1996 These results indicate that the M3-M4 loop is part of the ligand-binding pocket of the NR1 subunit and provide the basis for a refined model of the glycine-binding site of the NMDA receptor. Glycine 148-155 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 87-90 7903167-4 1993 By performing glycine concentration-response curves and comparing EC50s, it was possible to show that the NR1 + NR2A + NR2C receptor preferentially co-assembled when all three subunit cDNAs were present. Glycine 14-21 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 106-109 7870047-0 1995 Identification of amino acids in the N-methyl-D-aspartate receptor NR1 subunit that contribute to the glycine binding site. Glycine 102-109 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 67-70 7870047-4 1995 We have used site-directed mutagenesis to study amino acids in the human NR1 subunit that contribute to the glycine binding site of the NMDA receptor without affecting the agonist site for glutamate. Glycine 108-115 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 73-76 8011339-2 1994 Site-directed mutagenesis of the NMDAR1 (NR1) subunit revealed that aromatic residues at positions 390, 392, and 466 are crucial determinants of glycine binding. Glycine 145-152 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 33-39 8011339-2 1994 Site-directed mutagenesis of the NMDAR1 (NR1) subunit revealed that aromatic residues at positions 390, 392, and 466 are crucial determinants of glycine binding. Glycine 145-152 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 41-44 8613724-5 1995 The NMDA receptor modulators glycine and spermidine enhanced glutamate-mediated toxicity whereas ifenprodil potently and completely inhibited toxicity suggesting that the toxic response is mediated by the NR1/NR2B combination of NMDA subunits. Glycine 29-36 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 205-208 7528680-6 1994 The glycine site antagonist [3H]5,7-dichlorokynurenate bound with good affinity to all recombinant receptors (Kd approximately 50-100 nM), while glycine exhibited an affinity order of NR1-NR2C >> NR1 = NR1-NR2B = NR1-NR2D > NR1-NR2A. Glycine 4-11 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 184-187 7528680-6 1994 The glycine site antagonist [3H]5,7-dichlorokynurenate bound with good affinity to all recombinant receptors (Kd approximately 50-100 nM), while glycine exhibited an affinity order of NR1-NR2C >> NR1 = NR1-NR2B = NR1-NR2D > NR1-NR2A. Glycine 4-11 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 202-205 7528680-6 1994 The glycine site antagonist [3H]5,7-dichlorokynurenate bound with good affinity to all recombinant receptors (Kd approximately 50-100 nM), while glycine exhibited an affinity order of NR1-NR2C >> NR1 = NR1-NR2B = NR1-NR2D > NR1-NR2A. Glycine 4-11 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 202-205 7528680-6 1994 The glycine site antagonist [3H]5,7-dichlorokynurenate bound with good affinity to all recombinant receptors (Kd approximately 50-100 nM), while glycine exhibited an affinity order of NR1-NR2C >> NR1 = NR1-NR2B = NR1-NR2D > NR1-NR2A. Glycine 4-11 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 202-205 7528680-6 1994 The glycine site antagonist [3H]5,7-dichlorokynurenate bound with good affinity to all recombinant receptors (Kd approximately 50-100 nM), while glycine exhibited an affinity order of NR1-NR2C >> NR1 = NR1-NR2B = NR1-NR2D > NR1-NR2A. Glycine 4-11 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 202-205 7528680-6 1994 The glycine site antagonist [3H]5,7-dichlorokynurenate bound with good affinity to all recombinant receptors (Kd approximately 50-100 nM), while glycine exhibited an affinity order of NR1-NR2C >> NR1 = NR1-NR2B = NR1-NR2D > NR1-NR2A. Glycine 145-152 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 184-187 7903167-5 1993 This receptor had an affinity for glycine intermediate between that of NR1 + NR2A and NR1 + NR2C, but a similar Hill coefficient. Glycine 34-41 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 71-74 25659913-4 2015 Here, using BSP-SLIM method, a novel binding site within the core of spiral beta-strands-1-5 of LBD-GLUN1 has been predicted in glycine-bound GLUN1 conformation in addition to the glycine pocket in Apo-GLUN1. Glycine 128-135 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 100-105 7685113-4 1993 Oocytes injected with cRNA synthesized from the hNR1 cDNA express glutamate and NMDA-activated currents in the presence of glycine. Glycine 123-130 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 48-52 1397309-2 1992 In the NMDAR1 subunit, the signal of agonist binding may be carried from Y456 to W590 through an electron transport chain, including W480 which could be the glycine modulatory site. Glycine 157-164 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 7-13 33773999-6 2021 At the functional level, we found that GluN1-M641I/GluN2 and GluN1-A645S/GluN2 receptors expressed in HEK293 cells have wild-type EC50 values for both glutamate and glycine; in contrast, GluN1-Y647S/GluN2 receptors do not produce glutamate-induced currents. Glycine 165-172 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 39-44 33773999-6 2021 At the functional level, we found that GluN1-M641I/GluN2 and GluN1-A645S/GluN2 receptors expressed in HEK293 cells have wild-type EC50 values for both glutamate and glycine; in contrast, GluN1-Y647S/GluN2 receptors do not produce glutamate-induced currents. Glycine 165-172 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 61-66 33773999-6 2021 At the functional level, we found that GluN1-M641I/GluN2 and GluN1-A645S/GluN2 receptors expressed in HEK293 cells have wild-type EC50 values for both glutamate and glycine; in contrast, GluN1-Y647S/GluN2 receptors do not produce glutamate-induced currents. Glycine 165-172 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 61-66 25659913-8 2015 All these results suggest that nefiracetam can favorably complete with glycine for GLUN1-LBD in a two-step process, first by binding to a novel site of GLUN1-LBD-NMDA receptor followed by disruption of glycine-binding dynamics then replacing glycine in the GLUN1-LBD cleft. Glycine 71-78 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 83-88 25659913-8 2015 All these results suggest that nefiracetam can favorably complete with glycine for GLUN1-LBD in a two-step process, first by binding to a novel site of GLUN1-LBD-NMDA receptor followed by disruption of glycine-binding dynamics then replacing glycine in the GLUN1-LBD cleft. Glycine 71-78 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 152-157 25659913-8 2015 All these results suggest that nefiracetam can favorably complete with glycine for GLUN1-LBD in a two-step process, first by binding to a novel site of GLUN1-LBD-NMDA receptor followed by disruption of glycine-binding dynamics then replacing glycine in the GLUN1-LBD cleft. Glycine 71-78 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 152-157 25659913-4 2015 Here, using BSP-SLIM method, a novel binding site within the core of spiral beta-strands-1-5 of LBD-GLUN1 has been predicted in glycine-bound GLUN1 conformation in addition to the glycine pocket in Apo-GLUN1. Glycine 128-135 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 142-147 25659913-4 2015 Here, using BSP-SLIM method, a novel binding site within the core of spiral beta-strands-1-5 of LBD-GLUN1 has been predicted in glycine-bound GLUN1 conformation in addition to the glycine pocket in Apo-GLUN1. Glycine 128-135 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 142-147 25659913-4 2015 Here, using BSP-SLIM method, a novel binding site within the core of spiral beta-strands-1-5 of LBD-GLUN1 has been predicted in glycine-bound GLUN1 conformation in addition to the glycine pocket in Apo-GLUN1. Glycine 180-187 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 100-105 25659913-4 2015 Here, using BSP-SLIM method, a novel binding site within the core of spiral beta-strands-1-5 of LBD-GLUN1 has been predicted in glycine-bound GLUN1 conformation in addition to the glycine pocket in Apo-GLUN1. Glycine 180-187 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 142-147 25659913-4 2015 Here, using BSP-SLIM method, a novel binding site within the core of spiral beta-strands-1-5 of LBD-GLUN1 has been predicted in glycine-bound GLUN1 conformation in addition to the glycine pocket in Apo-GLUN1. Glycine 180-187 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 142-147 25659913-5 2015 Within the core of spiral beta-strands-1-5 of LBD-GLUN1 pocket, all-atom molecular dynamics simulation revealed that nefiracetam disrupts Arg523-glycine-Asp732 interaction resulting in open GLUN1 conformation and ultimate diffusion of glycine out of the clamshell cleft. Glycine 145-152 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 50-55 25659913-5 2015 Within the core of spiral beta-strands-1-5 of LBD-GLUN1 pocket, all-atom molecular dynamics simulation revealed that nefiracetam disrupts Arg523-glycine-Asp732 interaction resulting in open GLUN1 conformation and ultimate diffusion of glycine out of the clamshell cleft. Glycine 235-242 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 50-55 34736958-2 2022 It is now established that many NMDA receptors in the nervous system are triheteromeric, composed of two glycine-binding GluN1 subunits and two different glutamate binding GluN2 subunits. Glycine 105-112 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 121-126 34918931-2 2022 Here, we describe the design and synthesis of a series of (R)-3-(5-furanyl)carboxamido-2-aminopropanoic acid analogues 8a-s as agonists at the glycine (Gly) binding site in the GluN1 subunit, but not GluN3 subunits, of NMDA receptors. Glycine 143-150 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 177-182 34918931-2 2022 Here, we describe the design and synthesis of a series of (R)-3-(5-furanyl)carboxamido-2-aminopropanoic acid analogues 8a-s as agonists at the glycine (Gly) binding site in the GluN1 subunit, but not GluN3 subunits, of NMDA receptors. Glycine 152-155 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 177-182 34986531-4 2021 Recently, accumulating evidences have revealed two types of GluN3-containing NMDAR: glutamate-gated GluN1/GluN2/GluN3 NMDAR and glycine-gated GluN1/GluN3 NMDAR. Glycine 128-135 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 142-147 34504293-7 2021 We uncover allosteric coupling within NMDA LBD hetero-dimers, where binding of L-glutamate to the GluN2A LBD stalls clamshell motions of the glycine-binding GluN1 LBD. Glycine 141-148 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 157-162 34413877-4 2021 NMDARs that contained the P532H within the glycine-binding domain of GluN1 with either the GluN2A or GluN2B subunits were evaluated for changes in their pharmacological and biophysical properties, which surprisingly revealed only modest changes in glycine potency but a significant decrease in glutamate potency, an increase in sensitivity to endogenous zinc inhibition, a decrease in response to maximally effective concentrations of agonists, a shortened synaptic-like response time course, a decreased channel open probability, and a reduced receptor cell surface expression. Glycine 43-50 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 69-74 34413877-4 2021 NMDARs that contained the P532H within the glycine-binding domain of GluN1 with either the GluN2A or GluN2B subunits were evaluated for changes in their pharmacological and biophysical properties, which surprisingly revealed only modest changes in glycine potency but a significant decrease in glutamate potency, an increase in sensitivity to endogenous zinc inhibition, a decrease in response to maximally effective concentrations of agonists, a shortened synaptic-like response time course, a decreased channel open probability, and a reduced receptor cell surface expression. Glycine 248-255 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 69-74 32610085-2 2020 NMDARs are heterotetramers composed of GluN1 and GluN2 subunits, which bind glycine and glutamate, respectively, to activate their ion channels. Glycine 76-83 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 39-44 34058193-6 2021 On "conventional" GluN1/GluN2 NMDA receptors, glycine (or D-serine) acts in concert with glutamate as a mandatory co-agonist to set the level of receptor activity. Glycine 46-53 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 18-23 34058193-8 2021 On "unconventional" GluN1/GluN3 NMDARs, glycine acts as the sole agonist directly triggering opening of excitatory glycinergic channels recently shown to be physiologically relevant. Glycine 40-47 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 20-25 33976221-2 2021 Receptor activation involves glycine- and glutamate-stabilized closure of the GluN1 and GluN2 subunit ligand binding domains that is allosterically regulated by the amino-terminal domain (ATD). Glycine 29-36 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 78-83 33976221-6 2021 Glycine binding to GluN1 has no detectable effect, but unlocks the receptor for activation so that glycine and glutamate together drive an altered activation trajectory that is consistent with ATD dimer separation and rotation. Glycine 0-7 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 19-24 33976221-6 2021 Glycine binding to GluN1 has no detectable effect, but unlocks the receptor for activation so that glycine and glutamate together drive an altered activation trajectory that is consistent with ATD dimer separation and rotation. Glycine 99-106 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 19-24 32389749-2 2020 Most native NMDA receptors are tetrameric assemblies of two glycine-binding GluN1 and two glutamate-binding GluN2 subunits. Glycine 60-67 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 76-81 32389749-3 2020 Co-assembly of the glycine-binding GluN1 with glycine-binding GluN3 subunits (GluN3A-B) creates glycine-activated receptors that possess strikingly different functional and pharmacological properties compared to GluN1/GluN2 NMDA receptors. Glycine 19-26 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 35-40 32389749-3 2020 Co-assembly of the glycine-binding GluN1 with glycine-binding GluN3 subunits (GluN3A-B) creates glycine-activated receptors that possess strikingly different functional and pharmacological properties compared to GluN1/GluN2 NMDA receptors. Glycine 19-26 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 212-217 32389749-3 2020 Co-assembly of the glycine-binding GluN1 with glycine-binding GluN3 subunits (GluN3A-B) creates glycine-activated receptors that possess strikingly different functional and pharmacological properties compared to GluN1/GluN2 NMDA receptors. Glycine 46-53 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 35-40 32389749-3 2020 Co-assembly of the glycine-binding GluN1 with glycine-binding GluN3 subunits (GluN3A-B) creates glycine-activated receptors that possess strikingly different functional and pharmacological properties compared to GluN1/GluN2 NMDA receptors. Glycine 46-53 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 35-40 32389749-7 2020 Furthermore, we demonstrate that EU1180-438 produces robust inhibition of glycine-activated current responses mediated by native GluN1/GluN3A receptors in hippocampal CA1 pyramidal neurons. Glycine 74-81 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 129-134 31987864-7 2020 PTC-174 increases potencies of co-agonists glutamate and glycine by 2- to 5-fold at GluN1/2C and GluN1/2D receptors, and NMDA receptor activation facilitates allosteric modulation by PTC-174. Glycine 57-64 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 84-89 34321660-4 2021 Here we describe the cryo-electron microscope structures of human GluN1-GluN2A and GluN1-GluN2B NMDA receptors in complex with S-ketamine, glycine and glutamate. Glycine 139-146 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 66-71 34321660-4 2021 Here we describe the cryo-electron microscope structures of human GluN1-GluN2A and GluN1-GluN2B NMDA receptors in complex with S-ketamine, glycine and glutamate. Glycine 139-146 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 83-88 34201404-6 2021 The consequential changes in extracellular glycine concentration can lead to parallel changes in the activity of NR1/NR2B type NMDA receptors of which glycine is a mandatory agonist, and thereby may reduce neurodegenerative events in the retina. Glycine 43-50 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 113-116 34201404-6 2021 The consequential changes in extracellular glycine concentration can lead to parallel changes in the activity of NR1/NR2B type NMDA receptors of which glycine is a mandatory agonist, and thereby may reduce neurodegenerative events in the retina. Glycine 151-158 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 113-116 34201404-9 2021 We have hypothesized that glycine transporter 1 inhibitors and P2Y purinoceptor agonists may have therapeutic importance in neurodegenerative-neuroinflammatory disorders of the retina by decreasing NR1/NR2B NMDA receptor activity and production and release of a series of proinflammatory cytokines from microglial cells. Glycine 26-33 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 198-201 35217385-1 2022 N-methyl-D-aspartate receptors (NMDAR) are di- or tri-heterotetrameric ligand-gated ion channels composed of two obligate glycine-binding GluN1 subunits and two glutamate-binding GluN2 or GluN3 subunits, encoded by GRIN1, GRIN2A-D, and GRIN3A-B receptor genes respectively. Glycine 122-129 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 138-143 35217385-1 2022 N-methyl-D-aspartate receptors (NMDAR) are di- or tri-heterotetrameric ligand-gated ion channels composed of two obligate glycine-binding GluN1 subunits and two glutamate-binding GluN2 or GluN3 subunits, encoded by GRIN1, GRIN2A-D, and GRIN3A-B receptor genes respectively. Glycine 122-129 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 215-220 33098865-3 2020 Using single molecule FRET investigations, we show that in the presence of calcium-calmodulin the distance across the two GluN1 subunits at the entrance of the first transmembrane segment is shorter, and the bi-lobed cleft of the glycine-binding domain in GluN1 is more closed when bound to glycine and glutamate, relative to what is observed in the presence of barium-calmodulin. Glycine 230-237 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 122-127 33098865-3 2020 Using single molecule FRET investigations, we show that in the presence of calcium-calmodulin the distance across the two GluN1 subunits at the entrance of the first transmembrane segment is shorter, and the bi-lobed cleft of the glycine-binding domain in GluN1 is more closed when bound to glycine and glutamate, relative to what is observed in the presence of barium-calmodulin. Glycine 230-237 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 256-261 33098865-3 2020 Using single molecule FRET investigations, we show that in the presence of calcium-calmodulin the distance across the two GluN1 subunits at the entrance of the first transmembrane segment is shorter, and the bi-lobed cleft of the glycine-binding domain in GluN1 is more closed when bound to glycine and glutamate, relative to what is observed in the presence of barium-calmodulin. Glycine 291-298 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 122-127 33122756-3 2020 We found that the S688Y mutation significantly increases the EC50 of both glycine and D-serine in GluN1/GluN2A and GluN1/GluN2B receptors, and significantly slows desensitisation of GluN1/GluN3A receptors. Glycine 74-81 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 98-103 33122756-3 2020 We found that the S688Y mutation significantly increases the EC50 of both glycine and D-serine in GluN1/GluN2A and GluN1/GluN2B receptors, and significantly slows desensitisation of GluN1/GluN3A receptors. Glycine 74-81 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 115-120 33122756-3 2020 We found that the S688Y mutation significantly increases the EC50 of both glycine and D-serine in GluN1/GluN2A and GluN1/GluN2B receptors, and significantly slows desensitisation of GluN1/GluN3A receptors. Glycine 74-81 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 115-120 28760974-2 2017 Most NMDA receptors comprise two glycine-binding GluN1 and two glutamate-binding GluN2 subunits (GluN2A-D). Glycine 33-40 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 49-54 32048268-1 2020 BACKGROUND: N-methyl-D-aspartate (NMDA) receptor is a tetrameric protein complex composed of glycine-linked NR1 subunits and glutamate-linked NR2 subunits. Glycine 93-100 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 108-111 30482727-6 2019 Comparing across iGluR subtypes, these results are similar to glycine-binding GluN1 and GluN3A NMDA subunits and differ from glutamate-binding GluA2 and GluN2A subunits. Glycine 62-69 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 78-83 30139821-0 2018 Correction to "Identification of AICP as a GluN2C-Selective N-Methyl-D-Aspartate Receptor Superagonist at the GluN1 Glycine Site". Glycine 116-123 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 110-115 29917241-5 2018 ABSTRACT: NMDA receptors (NMDARs) are tetrameric complexes comprising two glycine-binding GluN1 and two glutamate-binding GluN2 subunits. Glycine 74-81 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 90-95 29887499-3 2018 Here, we investigate the process of agonist binding to the GluN2A (glutamate binding) and GluN1 (glycine binding) NMDA receptor subtypes using long-timescale unbiased molecular dynamics simulations. Glycine 97-104 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 90-95 29887499-6 2018 Glycine, on the other hand, binds to the GluN1 LBD via an "unguided-diffusion" mechanism, whereby glycine finds its binding site primarily by random thermal fluctuations. Glycine 0-7 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 41-46 29887499-6 2018 Glycine, on the other hand, binds to the GluN1 LBD via an "unguided-diffusion" mechanism, whereby glycine finds its binding site primarily by random thermal fluctuations. Glycine 98-105 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 41-46 29966365-2 2018 NR1 and NR3 subunits bind glycine, while NR2 subunits bind glutamate for full activation. Glycine 26-33 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 0-3 31302238-7 2019 This pathological overactivation of NR1/NR2B receptors can be reduced by GlyT-1 inhibitors (NFPS, Org-25935), which decrease excessive glycine release from astroglial cells or by selective antagonists of NR2B subunits (ifenprodil, Ro 25-6981). Glycine 135-142 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 36-39 31202607-3 2019 Importantly, GluN1/GluN3A and GluN1/GluN3B receptors form glycine-gated receptors. Glycine 58-65 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 13-18 31202607-3 2019 Importantly, GluN1/GluN3A and GluN1/GluN3B receptors form glycine-gated receptors. Glycine 58-65 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 30-35 31444392-0 2019 Structural features in the glycine-binding sites of the GluN1 and GluN3A subunits regulate the surface delivery of NMDA receptors. Glycine 27-34 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 56-61 31444392-3 2019 Here, we examined the surface delivery and functional properties of NMDARs containing mutations in the glycine-binding sites in GluN1 and GluN3A subunits expressed in mammalian cell lines and primary rat hippocampal neurons. Glycine 103-110 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 128-133 29681798-8 2018 We observed the most prominent effect when residues GluN1(L657) and GluN2B(I655) were deleted or altered to glycine. Glycine 108-115 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 52-57 28277064-7 2017 Platelet effects of a mouse monoclonal antibody targeting the glycine-binding region of GluN1 (GluN1-S2) were tested in assays of platelet activation, aggregation and thrombus formation. Glycine 62-69 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 88-93 28277064-7 2017 Platelet effects of a mouse monoclonal antibody targeting the glycine-binding region of GluN1 (GluN1-S2) were tested in assays of platelet activation, aggregation and thrombus formation. Glycine 62-69 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 95-103 28277064-12 2017 The epitope of anti-GluN1-S2 was mapped to alpha-helix H located within the glycine-binding clamshell of GluN1, where the antibody binding was computationally predicted to impair opening of the NMDAR channel. Glycine 76-83 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 20-28 28277064-12 2017 The epitope of anti-GluN1-S2 was mapped to alpha-helix H located within the glycine-binding clamshell of GluN1, where the antibody binding was computationally predicted to impair opening of the NMDAR channel. Glycine 76-83 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 20-25 28262924-3 2017 D-serine and glycine are coagonists of N-methyl-D-aspartate (NMDA) receptor subunit GRIN1. Glycine 13-20 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 84-89 28514141-3 2017 In particular, compounds 15a and 16a are potent GluN2C-specific superagonists at the GluN1 subunit with agonist efficacies of 398% and 308% compared to glycine. Glycine 152-159 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 85-90 28365212-1 2017 N-methyl-d-aspartate (NMDA) receptors assembled from GluN1 and GluN3 subunits are unique in that they form glycine-gated excitatory channels that are insensitive to glutamate and NMDA. Glycine 107-114 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 53-58 28468946-4 2017 In this study, we present the crystal structure of the isolated ligand-binding domain of the GluN1-GluN2A NMDA receptor in complex with the GluN1 agonist glycine and the GluN2A antagonist NVP-AAM077. Glycine 154-161 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 93-98 28468946-4 2017 In this study, we present the crystal structure of the isolated ligand-binding domain of the GluN1-GluN2A NMDA receptor in complex with the GluN1 agonist glycine and the GluN2A antagonist NVP-AAM077. Glycine 154-161 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 140-145 28588066-0 2017 Identification of AICP as a GluN2C-Selective N-Methyl-d-Aspartate Receptor Superagonist at the GluN1 Glycine Site. Glycine 101-108 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 95-100 28588066-8 2017 We show that GluN1/2C superagonism of AICP and DCS is mediated by overlapping but distinct mechanisms and that AICP selectively enhances responses from recombinant GluN1/2C receptors in the presence of physiological glycine concentrations. Glycine 216-223 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 164-169 28228639-5 2017 GluN1-G620R/GluN2A complexes showed a mild reduction in trafficking, a ~2-fold decrease in glutamate and glycine potency, a strong decrease in sensitivity to Mg2+ block, and a significant reduction of current responses to a maximal effective concentration of agonists. Glycine 105-112 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 0-5 28378791-7 2017 To validate this prediction, we perform electrophysiological analysis of full-length NMDARs with a glycosylation-preventing GluN1-N440Q mutation, and demonstrate an increase in the glycine EC50 value. Glycine 181-188 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 124-129 28534738-5 2017 PSAA photoisomerization at the GluN1 clamshell hinge is sufficient to control glycine sensitivity and activation efficacy. Glycine 78-85 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 31-36 27270213-6 2016 Single-channel patch-clamp and four-channel fluorescence measurement are recorded simultaneously to get correlation among electrical on and off states, optically determined conformational open and closed states by FRET, and binding-unbinding states of the glycine ligand by anisotropy measurement at the ligand binding domain of GluN1 subunit. Glycine 256-263 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 329-334 28059133-1 2017 The glycine-binding site of the N-methyl-D-aspartate receptor (NMDAR) subunit GluN1 is a potential pharmacological target for neurodegenerative disorders. Glycine 4-11 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 78-83 27618671-4 2016 NAM binding causes displacement of a valine in GluN2A and the resulting steric effects can be mitigated by the transition from glycine bound to apo state of the GluN1 LBD. Glycine 127-134 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 161-166 27010645-5 2016 KEY RESULTS: Six pairs of positions in GluN1/GluN2B significantly interacted to regulate ethanol inhibition: Gly(638) /Met(824) , Gly(638) /Leu(825) , Phe(639) /Leu(825) , Phe(639) /Gly(826) , Met(818) /Phe(637) and Val(820) /Phe(637) . Glycine 109-112 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 39-44 27010645-5 2016 KEY RESULTS: Six pairs of positions in GluN1/GluN2B significantly interacted to regulate ethanol inhibition: Gly(638) /Met(824) , Gly(638) /Leu(825) , Phe(639) /Leu(825) , Phe(639) /Gly(826) , Met(818) /Phe(637) and Val(820) /Phe(637) . Glycine 130-133 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 39-44 27010645-5 2016 KEY RESULTS: Six pairs of positions in GluN1/GluN2B significantly interacted to regulate ethanol inhibition: Gly(638) /Met(824) , Gly(638) /Leu(825) , Phe(639) /Leu(825) , Phe(639) /Gly(826) , Met(818) /Phe(637) and Val(820) /Phe(637) . Glycine 130-133 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 39-44 26577016-7 2016 Glycine substitution in the GluN1 S2-M4 region significantly decreased glutamate potency of GluN1(A804G)/GluN2A receptors, while GluN1(A804G)/GluN2B receptors exhibited no change in glutamate sensitivity. Glycine 0-7 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 28-33 26577016-7 2016 Glycine substitution in the GluN1 S2-M4 region significantly decreased glutamate potency of GluN1(A804G)/GluN2A receptors, while GluN1(A804G)/GluN2B receptors exhibited no change in glutamate sensitivity. Glycine 0-7 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 92-97 26577016-7 2016 Glycine substitution in the GluN1 S2-M4 region significantly decreased glutamate potency of GluN1(A804G)/GluN2A receptors, while GluN1(A804G)/GluN2B receptors exhibited no change in glutamate sensitivity. Glycine 0-7 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 92-97 26661043-4 2016 Here, we investigate the pharmacology of the orthosteric binding site in GluD2 by examining the activity of analogs of D-Ser and GluN1 glycine site competitive antagonists at GluD2 receptors containing the lurcher mutation (GluD2(LC)), which promotes spontaneous channel activation. Glycine 135-142 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 129-134 27000430-3 2016 Uniquely within the NMDA receptor family, GluN1/GluN3 receptors produce glycine-gated deeply desensitising currents that are insensitive to glutamate and NMDA; these currents remain poorly characterised and their cellular functions are unknown. Glycine 72-79 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 42-47 27000430-4 2016 Here, we show that extracellular acidification strongly potentiated glycine-gated currents from recombinant GluN1/GluN3A receptors, with half-maximal effect in the physiologic pH range. Glycine 68-75 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 108-113 25817860-2 2015 NMDA receptors are a tetramer that consists of two glycine-binding subunits GluN1, two glutamate-binding subunits (i.e., GluN2A, GluN2B, GluN2C, and GluN2D), a combination of a GluN2 subunit and glycine-binding GluN3 subunit (i.e., GluN3A or GluN3B), or two GluN3 subunits. Glycine 51-58 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 76-81 25964432-5 2015 We examined currents recorded from cell-attached patches containing one GluN1/GluN2A receptor in the presence of several glycine-site agonists and used kinetic modeling of these data to develop reaction schemes that include explicit glycine-binding steps. Glycine 233-240 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 72-77 25964432-7 2015 These results complete the basic steps of an NMDA receptor reaction scheme for the GluN1/GluN2A isoform and prompt a reevaluation of how glycine controls NMDA receptor activation. Glycine 137-144 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 83-88 25544544-4 2015 We show herein that the ligand binding domains (LBD) of the GluN1 and GluN2A subunits of the NMDAR heterodimerize only when both coagonists, Glu and Gly/d-Ser, bind to their respective sites on GluN2 and GluN1. Glycine 149-152 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 204-209 25544544-6 2015 Also, in a heteromer formed by the LBDs, GluN2A is more sensitized to bind Glu, while the affinity of Gly for GluN1 remains unchanged. Glycine 102-105 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 110-115 25339225-3 2015 We found that the apparent affinity of glycine to GluN1 (K gly ~ 0.6 muM) is much higher than NMDA or glutamate to GluN2 (K NMDA ~ 36 muM, K glu ~ 4.8 muM). Glycine 39-46 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 50-55 25339225-3 2015 We found that the apparent affinity of glycine to GluN1 (K gly ~ 0.6 muM) is much higher than NMDA or glutamate to GluN2 (K NMDA ~ 36 muM, K glu ~ 4.8 muM). Glycine 39-42 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 50-55 25339225-4 2015 The binding rate constant (derived from the linear regression of the apparent macroscopic binding rates) of glycine to GluN1 (~9.8 x 10(6) M(-1) s(-1)), however, is only slightly faster than NMDA to GluN2 (~4.1 x 10(6) M(-1) s(-1)). Glycine 108-115 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 119-124 25339225-5 2015 Accordingly, the apparent unbinding rates of glycine from activated GluN1 (time constant ~2 s) are much slower than NMDA from activated GluN2 (time constant ~70 ms). Glycine 45-52 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 68-73 25339225-10 2015 Moreover, specific mutations involving A7 in GluN1 but not in GluN2 result in channels showing markedly enhanced affinity to both glycine and NMDA and readily activated by only NMDA, as if the channel is already partially activated. Glycine 130-137 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 45-50 26086092-3 2015 It was found that polyamines, especially spermidine, can permeate NMDA channels expressed from GluN1/GluN2A or GluN1/GluN2B activated by glycine and glutamate. Glycine 137-144 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 95-100 26086092-3 2015 It was found that polyamines, especially spermidine, can permeate NMDA channels expressed from GluN1/GluN2A or GluN1/GluN2B activated by glycine and glutamate. Glycine 137-144 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 111-116 25544544-4 2015 We show herein that the ligand binding domains (LBD) of the GluN1 and GluN2A subunits of the NMDAR heterodimerize only when both coagonists, Glu and Gly/d-Ser, bind to their respective sites on GluN2 and GluN1. Glycine 149-152 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 60-65 26205290-4 2015 Inhibition of GlyT1 reduces clearance of extra-cellular glycine near NMDA receptor-containing synapses, and thereby increases baseline occupancy of the glycine-B site at the NR1 subunit of the NMDA receptor, which is a prerequisite of channel activation upon stimulation by the excitatory neurotransmitter glutamate. Glycine 152-159 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 174-177 25017909-1 2014 Unlike GluN2-containing N-methyl-d-aspartate (NMDA) receptors, which require both glycine and glutamate for activation, receptors composed of GluN1 and GluN3 subunits are activated by glycine alone. Glycine 184-191 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 142-147 25205677-4 2014 Coapplication of 50 muM PYD-106 with a maximally effective concentration of glutamate and glycine increases the response of GluN1/GluN2C NMDA receptors in HEK-293 cells to 221% of that obtained in the absence of PYD (taken as 100%). Glycine 90-97 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 124-129 25017909-4 2014 Isolated GluN1/GluN3A receptors integrated into lipid bilayers responded to addition of either glycine or d-serine, but not glutamate, with a ~1 nm reduction in height of the extracellular domain. Glycine 95-102 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 9-14 23077649-4 2012 While the binding of a full agonist glycine to LBD of GluN1 is linked to cleft closure and subsequent ion-channel opening, partial agonists are known to activate the receptor only sub-maximally. Glycine 36-43 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 54-59 22814002-5 2012 Pharmacology revealed a triheteromeric-receptor with features common to glutamate-activated GluN1/GluN2-containing and glycine-activated GluN1/GluN3-containing diheteromeric NMDARs. Glycine 119-126 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 137-142 22812023-5 2004 In terms of agonist requirement and channel operation, the three subunit families exhibit distinct properties; NR1 and NR3 require glycine as the agonist and have no binding site for glutamate, whereas NR2 is activated by glutamate. Glycine 131-138 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 111-114 22812023-6 2004 Opening of the ion channel is dependent on the voltage state of the cell membrane as well as the binding of dual ligands; glutamate binds to a site on the NR2 subunit, and glycine or d-serine binds to a modulatory site on the NR1 subunit (2, 4). Glycine 172-179 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 226-229 23973313-1 2013 NMDA receptors are ligand-gated ion channels that assemble into tetrameric receptor complexes composed of glycine-binding GluN1 and GluN3 subunits (GluN3A-B) and glutamate-binding GluN2 subunits (GluN2A-D). Glycine 106-113 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 122-127 23973313-2 2013 NMDA receptors can assemble as GluN1/N2 receptors and as GluN3-containing NMDA receptors, which are either glutamate/glycine-activated triheteromeric GluN1/N2/N3 receptors or glycine-activated diheteromeric GluN1/N3 receptors. Glycine 117-124 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 150-155 23973313-2 2013 NMDA receptors can assemble as GluN1/N2 receptors and as GluN3-containing NMDA receptors, which are either glutamate/glycine-activated triheteromeric GluN1/N2/N3 receptors or glycine-activated diheteromeric GluN1/N3 receptors. Glycine 117-124 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 150-155 23973313-3 2013 The glycine-binding GluN1 and GluN3 subunits display strikingly different pharmacological selectivity profiles. Glycine 4-11 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 20-25 23972471-2 2013 GluN1 and GluN3 bind glycine, whereas GluN2 binds glutamate. Glycine 21-28 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 0-5 23962100-13 2013 The NMDA subunits NR2b and NR2a, in addition to the N-terminal region of the glycine binding NR1 subunit, have been implicated. Glycine 77-84 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 93-96 23909910-2 2013 Several members of this class inhibit NMDA receptor responses in the nanomolar range and are more than 50-fold selective over GluN1/GluN2A and GluN1/GluN2B NMDA receptors, as well as AMPA, kainate, GABA, glycine, nicotinic, serotonin, and purinergic receptors. Glycine 204-211 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 126-131 23909910-2 2013 Several members of this class inhibit NMDA receptor responses in the nanomolar range and are more than 50-fold selective over GluN1/GluN2A and GluN1/GluN2B NMDA receptors, as well as AMPA, kainate, GABA, glycine, nicotinic, serotonin, and purinergic receptors. Glycine 204-211 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 143-148 23941530-0 2013 Identification of a single amino acid in GluN1 that is critical for glycine-primed internalization of NMDA receptors. Glycine 68-75 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 41-46 23941530-4 2013 RESULTS: Here we address the key issue of identifying molecular determinants in the glycine-binding subunit, GluN1, that are essential for priming of NMDA receptors. Glycine 84-91 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 109-114 23941530-6 2013 However, with a glycine-binding mutant of GluN1 - N710R/Y711R/E712A/A714L - we found that treating with glycine did not promote recruitment of AP-2 nor were glycine-treated receptors internalized when subsequently activated with NMDA plus glycine. Glycine 16-23 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 42-47 23941530-6 2013 However, with a glycine-binding mutant of GluN1 - N710R/Y711R/E712A/A714L - we found that treating with glycine did not promote recruitment of AP-2 nor were glycine-treated receptors internalized when subsequently activated with NMDA plus glycine. Glycine 104-111 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 42-47 23941530-6 2013 However, with a glycine-binding mutant of GluN1 - N710R/Y711R/E712A/A714L - we found that treating with glycine did not promote recruitment of AP-2 nor were glycine-treated receptors internalized when subsequently activated with NMDA plus glycine. Glycine 104-111 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 42-47 23941530-6 2013 However, with a glycine-binding mutant of GluN1 - N710R/Y711R/E712A/A714L - we found that treating with glycine did not promote recruitment of AP-2 nor were glycine-treated receptors internalized when subsequently activated with NMDA plus glycine. Glycine 104-111 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 42-47 23941530-9 2013 CONCLUSIONS: Thus, we have identified a single amino acid in GluN1 that is critical for priming of NMDA receptors by glycine. Glycine 117-124 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 61-66 23116391-1 2013 Over the years, accumulating evidence has indicated that D-serine represents the endogenous ligand for the glycine modulatory binding site on the NR1 subunit of N-methyl-D-aspartate receptors in various brain areas. Glycine 107-114 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 146-149 22715100-5 2012 In single-substitution mutants, we found that a position in both subunits adjacent to one previously identified, GluN1(Gly-638) and GluN2A(Phe-636), can strongly regulate ethanol sensitivity. Glycine 119-122 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 113-118 22715100-6 2012 Significant interactions affecting ethanol inhibition and receptor deactivation were observed at four pairs of positions in GluN1/GluN2A: Gly-638/Met-823, Phe-639/Leu-824, Met-818/Phe-636, and Leu-819/Phe-637; the latter pair also interacted with respect to desensitization. Glycine 138-141 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 124-129 22634870-8 2012 CONCLUSIONS: These findings confirm xenon binds to the glycine site of the GluN1 subunit of the NMDA receptor and indicate that interactions between xenon and the aromatic ring of the phenylalanine 758 residue are important for xenon binding. Glycine 55-62 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 75-80 21735122-3 2012 Our docking results show that the calculated pK (i) values of glycine and L: -glutamate significantly increase (>1) when the NR1 and NR2A S1S2 domains are closing, respectively. Glycine 62-69 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 125-128 20678516-3 2010 As glycine is an obligatory co-agonist at the NR1 subunit of the NMDA receptor, blockade of glycine uptake at the glycine transporter type-1 (GlyT1) can enhance low glutamatergic tone. Glycine 3-10 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 46-49 21746848-2 2011 NMDA receptors are obligate heterotetramers typically composed of glycine-binding GluN1 and glutamate-binding GluN2 subunits that gate in a concerted fashion, requiring all four ligands to bind for subsequent opening of the channel pore. Glycine 66-73 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 82-87 21454656-1 2011 The conformational changes in the agonist binding domain of the glycine-binding GluN1 and glutamate-binding GluN2A subunits of the N-methyl D-aspartic acid receptor upon binding agonists of varying efficacy have been investigated by luminescence resonance energy transfer (LRET) measurements. Glycine 64-71 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 80-85 20810618-1 2010 NR1/NR2A is a subtype of N-methyl-d-aspartate receptors (NMDARs), which are glutamate and glycine-gated Ca(2+)-permeable channels highly expressed in the central nervous system. Glycine 90-97 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 0-3 20810618-4 2010 Addition of 1 mM glycine, but not 1 mM l-glutamate, was able to surmount compound 1 and 13 inhibitory effects in FLIPR NR1/NR2A assay. Glycine 17-24 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 119-122 20678516-3 2010 As glycine is an obligatory co-agonist at the NR1 subunit of the NMDA receptor, blockade of glycine uptake at the glycine transporter type-1 (GlyT1) can enhance low glutamatergic tone. Glycine 92-99 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 46-49 20958962-8 2010 Ca2+ permeability could be rescued by mutating the NR3 N site glycine to the NR1-like asparagine. Glycine 62-69 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 77-80 20890276-2 2010 Two glycine-binding NR1 subunits and two glutamate-binding NR2 subunits each form highly Ca2(+)-permeable cation channels which are blocked by extracellular Mg2(+) in a voltage-dependent manner. Glycine 4-11 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 20-23 20958962-10 2010 Conversely, "conventional" receptors assembled from NR1 and NR2 could be made Mg2+ insensitive and Ca2+ impermeable by equipping either subunit with the NR3-like glycine at their N positions, with a stronger contribution of the NR1 subunit. Glycine 162-169 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 52-55 20958962-10 2010 Conversely, "conventional" receptors assembled from NR1 and NR2 could be made Mg2+ insensitive and Ca2+ impermeable by equipping either subunit with the NR3-like glycine at their N positions, with a stronger contribution of the NR1 subunit. Glycine 162-169 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 228-231 20844142-3 2010 Within the glutamate receptor family, NMDA-sensitive channels are unique in their requirement that both glycine and glutamate bind to homologous regions on GluN1 and GluN2 subunits, respectively, before the channel can open. Glycine 104-111 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 156-161 20097255-4 2010 While glutamate activates triheteromeric NMDARs composed of NR1/NR2/NR3A subunits, glycine is sufficient to activate diheteromeric NR1/NR3A-containing receptors. Glycine 83-90 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 131-134 20304927-2 2010 Typically, glycine binding NR1 subunits co-assemble with glutamate binding NR2 subunits to form a functional receptor. Glycine 11-18 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 27-30 20448042-4 2010 The N-methyl-D-aspartate (NMDA) receptor is composed of NR1 and NR2 subunits, which are activated by co-agonist glycine and glutamate or aspartate, respectively. Glycine 112-119 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 56-59 20448042-8 2010 Pharmacological and molecular inhibition of DVC NR1 negated the metabolic effect of glycine. Glycine 84-91 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 48-51 20195697-1 2010 Over the past years, accumulating evidence has indicated that D-serine is the endogenous ligand for the glycine-modulatory binding site on the NR1 subunit of N-methyl-D-aspartate receptors in various brain areas. Glycine 104-111 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 143-146 20407581-0 2010 Potentiation of Glycine-Gated NR1/NR3A NMDA Receptors Relieves Ca-Dependent Outward Rectification. Glycine 16-23 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 30-33 20407581-3 2010 Classical Ca(2+)-permeable NMDA receptors are composed of glycine-binding NR1 and glutamate-binding NR2 subunits, and hence require both glutamate and glycine for efficient activation. Glycine 58-65 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 74-77 20407581-3 2010 Classical Ca(2+)-permeable NMDA receptors are composed of glycine-binding NR1 and glutamate-binding NR2 subunits, and hence require both glutamate and glycine for efficient activation. Glycine 151-158 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 74-77 20407581-4 2010 In contrast, recombinant receptors composed of NR1 and the glycine binding NR3A and/or NR3B subunits lack glutamate binding sites and can be activated by glycine alone. Glycine 154-161 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 47-50 20407581-6 2010 Co-application of antagonists of the NR1 glycine-binding site or of the divalent cation Zn(2+) markedly enhances the glycine responses of these receptors. Glycine 41-48 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 37-40 20407581-6 2010 Co-application of antagonists of the NR1 glycine-binding site or of the divalent cation Zn(2+) markedly enhances the glycine responses of these receptors. Glycine 117-124 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 37-40 20407581-8 2010 Whole-cell current-voltage relations of glycine currents recorded from NR1/NR3B and NR1/NR3A/NR3B expressing oocytes were found to be linear under our recording conditions. Glycine 40-47 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 71-74 20407581-8 2010 Whole-cell current-voltage relations of glycine currents recorded from NR1/NR3B and NR1/NR3A/NR3B expressing oocytes were found to be linear under our recording conditions. Glycine 40-47 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 84-87 20164358-1 2010 We have studied relative efficacies of NR1 agonists glycine and d-cycloserine (DCS), and found efficacy to be dependent on the NR2 subunit. Glycine 52-59 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 39-42 20164358-2 2010 DCS shows partial agonism at NR1/NR2B but has higher relative efficacy than glycine at NR1/NR2C receptor. Glycine 76-83 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 87-90 19909274-2 2009 The differences are, to a large extent, determined by the identities of the GluN2 (glutamate-binding) NMDAR subunits that are co-expressed with GluN1 (glycine-binding) subunits, which form the final tetrameric NMDAR assembly. Glycine 151-158 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 144-149 19726695-6 2009 However, robust glycine-activated currents were generated in cells transfected with NR3(A or B) and either NR1-2a, NR1-3a, or NR1-4a, and current density was correlated with NR1 C-terminal length. Glycine 16-23 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 107-110 19726695-0 2009 Expression of glycine-activated diheteromeric NR1/NR3 receptors in human embryonic kidney 293 cells Is NR1 splice variant-dependent. Glycine 14-21 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 46-49 19726695-0 2009 Expression of glycine-activated diheteromeric NR1/NR3 receptors in human embryonic kidney 293 cells Is NR1 splice variant-dependent. Glycine 14-21 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 103-106 19726695-1 2009 In oocytes, glycine activates receptors formed by diheteromeric combinations of N-methyl-d-aspartate (NMDA) NR1 and NR3 subunits. Glycine 12-19 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 108-111 19726695-6 2009 However, robust glycine-activated currents were generated in cells transfected with NR3(A or B) and either NR1-2a, NR1-3a, or NR1-4a, and current density was correlated with NR1 C-terminal length. Glycine 16-23 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 115-118 19726695-6 2009 However, robust glycine-activated currents were generated in cells transfected with NR3(A or B) and either NR1-2a, NR1-3a, or NR1-4a, and current density was correlated with NR1 C-terminal length. Glycine 16-23 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 115-118 19726695-6 2009 However, robust glycine-activated currents were generated in cells transfected with NR3(A or B) and either NR1-2a, NR1-3a, or NR1-4a, and current density was correlated with NR1 C-terminal length. Glycine 16-23 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 115-118 19726695-8 2009 In contrast, large currents were observed when an extracellular phenylalanine in NR1-1a that influences glycine access was mutated to alanine. Glycine 104-111 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 81-84 19726695-9 2009 A separate mutation in NR1-1a that disrupts glycine binding did not generate responses in NR1-1a/NR3A receptors alone, but it produced a greater than 30-fold potentiation of currents during coapplication of glycine and the glycine antagonist 7-chlorokynurenic acid. Glycine 44-51 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 23-26 19726695-9 2009 A separate mutation in NR1-1a that disrupts glycine binding did not generate responses in NR1-1a/NR3A receptors alone, but it produced a greater than 30-fold potentiation of currents during coapplication of glycine and the glycine antagonist 7-chlorokynurenic acid. Glycine 207-214 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 23-26 19726695-9 2009 A separate mutation in NR1-1a that disrupts glycine binding did not generate responses in NR1-1a/NR3A receptors alone, but it produced a greater than 30-fold potentiation of currents during coapplication of glycine and the glycine antagonist 7-chlorokynurenic acid. Glycine 207-214 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 23-26 19487695-3 2009 Conventional NMDA receptors are obligatory heterotetramers composed of two glycine-binding NR1 subunits and two glutamate-binding NR2 subunits. Glycine 75-82 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 91-94 20641908-1 2004 The NMDA receptor forms a heterotetramer between two NR1 and two NR2 subunits with multiple regulatory binding sites for glutamate, glycine, Mg(2+), polyamine, and drugs such as phencyclidine (PCP) (2). Glycine 132-139 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 53-56 19243863-2 2009 We use as reference the glycine site in the NR1 subunit of the NMDA receptor (Glycine(B)-iGluR-NMDA). Glycine 24-31 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 44-47 18988464-2 2008 It was concluded that Gly, D-Ser, D-Asn and D-Thr are ligands of NR1-binding core native NMDA-receptor, whereas the chiral modified NR1-binding core is characterized by the aliphatic non-polar amino acids D-Ala, D-Leu, D-Ile and D-Pro as ligands. Glycine 22-25 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 65-68 19348678-6 2009 We provide evidence that functional excitatory glycine receptors formed regardless of the NR1 isoform, and their pharmacological profile matched the one reported for NR1-1a/NR3: glycine alone fully activated the receptors, which were insensitive to glutamate and block by Mg2+. Glycine 47-54 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 166-169 18779583-1 2008 Canonical NMDA receptors assemble from two glycine-binding NR1 subunits with two glutamate-binding NR2 subunits to form glutamate-gated excitatory receptors that mediate synaptic transmission and plasticity. Glycine 43-50 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 59-62 18711142-1 2008 Coassembly of the glycine-binding NMDA receptor subunits NR1 and NR3A results in excitatory glycine receptors of low efficacy. Glycine 18-25 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 57-60 18711142-2 2008 Here, we report that micromolar concentrations of the divalent cation Zn(2+) produce a 10-fold potentiation of NR1/NR3A receptor responses, which resembles that seen upon antagonizing glycine binding to the NR1 subunit. Glycine 184-191 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 111-114 18711142-2 2008 Here, we report that micromolar concentrations of the divalent cation Zn(2+) produce a 10-fold potentiation of NR1/NR3A receptor responses, which resembles that seen upon antagonizing glycine binding to the NR1 subunit. Glycine 184-191 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 207-210 18711142-3 2008 Coapplication of both Zn(2+) and NR1 antagonist caused a supralinear potentiation, resulting in a >120-fold increase of glycine-activated currents. Glycine 123-130 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 33-36 18711142-5 2008 Point mutations in the NR1 and NR3A glycine-binding sites revealed that both the potentiating and agonistic effects of Zn(2+) are mediated by the ligand-binding domain of the NR1 subunit. Glycine 36-43 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 175-178 18450751-4 2008 Two mutants, E522C/I691C in NR1 (EI) and K487C/N687C in NR2 (KN) were found to exhibit significant glycine- and glutamate-independent activation, respectively, and co-expression of the two subunits produced a constitutively active channel. Glycine 99-106 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 28-31 18635641-4 2008 NR1/NR2C receptors activated by a maximally effective concentration of glutamate and glycine had two main conductance levels of 45 pS and 28 pS when the extracellular Ca(2+) concentration was 0.5 mm and the holding potential was -80 mV. Glycine 85-92 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 0-3 18629001-6 2008 Recombinant NR1 glycine binding protein was used to identify MMP-3 cleavage sites within the extracellular S1 and S2-domains. Glycine 16-23 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 12-15 17959602-1 2008 N-Methyl-D-aspartate (NMDA) receptors are tetrameric protein complexes composed of the glycine-binding NR1 subunit with a glutamate-binding NR2 and/or glycine-binding NR3 subunit. Glycine 87-94 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 103-106 18068304-2 2008 These ligand-gated ion channels are heteromultimers composed of NR1 and NR2 subunits activated by glycine and glutamate. Glycine 98-105 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 64-67 17959602-2 2008 Tri-heteromeric receptors containing NR1, NR2, and NR3 subunits reconstitute channels, which differ strikingly in many properties from the respective glycine- and glutamate-gated NR1/NR2 complexes and the NR1/NR3 receptors gated by glycine alone. Glycine 232-239 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 37-40 17959602-2 2008 Tri-heteromeric receptors containing NR1, NR2, and NR3 subunits reconstitute channels, which differ strikingly in many properties from the respective glycine- and glutamate-gated NR1/NR2 complexes and the NR1/NR3 receptors gated by glycine alone. Glycine 232-239 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 179-182 17959602-2 2008 Tri-heteromeric receptors containing NR1, NR2, and NR3 subunits reconstitute channels, which differ strikingly in many properties from the respective glycine- and glutamate-gated NR1/NR2 complexes and the NR1/NR3 receptors gated by glycine alone. Glycine 232-239 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 179-182 17959602-2 2008 Tri-heteromeric receptors containing NR1, NR2, and NR3 subunits reconstitute channels, which differ strikingly in many properties from the respective glycine- and glutamate-gated NR1/NR2 complexes and the NR1/NR3 receptors gated by glycine alone. Glycine 150-157 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 37-40 17959602-2 2008 Tri-heteromeric receptors containing NR1, NR2, and NR3 subunits reconstitute channels, which differ strikingly in many properties from the respective glycine- and glutamate-gated NR1/NR2 complexes and the NR1/NR3 receptors gated by glycine alone. Glycine 150-157 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 179-182 17959602-2 2008 Tri-heteromeric receptors containing NR1, NR2, and NR3 subunits reconstitute channels, which differ strikingly in many properties from the respective glycine- and glutamate-gated NR1/NR2 complexes and the NR1/NR3 receptors gated by glycine alone. Glycine 150-157 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 179-182 18073551-3 2007 The authors show that xenon and isoflurane compete for the binding of the coagonist glycine on the NMDA receptor NR1 subunit. Glycine 84-91 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 113-116 17878266-0 2007 The N-terminal domains of both NR1 and NR2 subunits determine allosteric Zn2+ inhibition and glycine affinity of N-methyl-D-aspartate receptors. Glycine 93-100 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 31-34 17878266-1 2007 The N-methyl-D-aspartate (NMDA) subtype of ionotropic glutamate receptors (iGluRs) is a tetrameric protein composed of homologous NR1 and NR2 subunits, which require the binding of glycine and glutamate, respectively, for efficient channel gating. Glycine 181-188 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 130-133 17878266-7 2007 Furthermore, by replacing the NR2A-NTD with the NR2B NTD, and vice versa, the different glycine affinities of NR1/NR2A and NR1/NR2B receptors were found to be determined by their respective NR2-NTDs. Glycine 88-95 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 110-113 17878266-7 2007 Furthermore, by replacing the NR2A-NTD with the NR2B NTD, and vice versa, the different glycine affinities of NR1/NR2A and NR1/NR2B receptors were found to be determined by their respective NR2-NTDs. Glycine 88-95 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 123-126 17878266-8 2007 Together, these data show that the NTDs of both the NR1 and NR2 subunits determine allosteric inhibition and glycine potency but are not required for NMDA receptor assembly. Glycine 109-116 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 52-55 18073551-9 2007 The loss of inhibitory effect of xenon and isoflurane in mutant NR1(F639A)/NR2A receptors is explained by increased glycine affinity of the mutant receptors, and inhibition is restored at low glycine concentrations. Glycine 116-123 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 64-67 18073551-9 2007 The loss of inhibitory effect of xenon and isoflurane in mutant NR1(F639A)/NR2A receptors is explained by increased glycine affinity of the mutant receptors, and inhibition is restored at low glycine concentrations. Glycine 192-199 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 64-67 17502428-0 2007 Pharmacological characterization of glycine-activated currents in HEK 293 cells expressing N-methyl-D-aspartate NR1 and NR3 subunits. Glycine 36-43 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 112-115 17617428-5 2007 We have previously reported that NR3A contains a glycine binding site, with similar affinity as the glycine binding site of NR1 subunits. Glycine 100-107 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 124-127 17502428-7 2007 The NMDA receptor glycine site agonist, d-serine, partially activated NR1/NR3A/NR3B receptors, whereas the antagonist, 5,7-dichloro-kynurenic acid, inhibited receptor currents. Glycine 18-25 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 70-73 17047094-0 2007 Subunit-specific roles of glycine-binding domains in activation of NR1/NR3 N-methyl-D-aspartate receptors. Glycine 26-33 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 67-70 17214961-1 2007 Calcium-permeable N-methyl-d-aspartate (NMDA) receptors are tetrameric cation channels composed of glycine-binding NR1 and glutamate-binding NR2 subunits, which require binding of both glutamate and glycine for efficient channel gating. Glycine 99-106 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 115-118 17320117-4 2007 The NMDA NR1 glycine site agonist d-serine and partial agonist HA-966 (3-amino-1-hydroxypyrrolid-2-one), similarly to glycine displaced [(3)H]-glycine monophasically, suggesting a single common binding site. Glycine 13-20 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 9-12 17050777-7 2007 AQ-tetraamines could permeate the channel at very negative membrane potentials when the narrowest constriction of the channel was expanded by replacing the Asn residue at Asn616 of NR1 and NR2B with Gly, whereas Ant-tetraamines did not easily pass through the channel, apparently because of differences in the relative position of the head groups on AQ- and Ant-polyamines. Glycine 199-202 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 181-184 17403555-9 2007 Stimulation of NR1/NR2A receptors with NMDA/glycine revealed an increase in intracellular calcium in cells pre-exposed to Abeta(1-40). Glycine 44-51 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 15-18 17214961-3 2007 Here, we show that antagonists of and substitutions within the glycine-binding site of NR1 potentiate NR1/NR3 receptor function up to 25-fold, but inhibition or mutation of the NR3 glycine binding site reduces or abolishes receptor activation. Glycine 63-70 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 87-90 17214961-3 2007 Here, we show that antagonists of and substitutions within the glycine-binding site of NR1 potentiate NR1/NR3 receptor function up to 25-fold, but inhibition or mutation of the NR3 glycine binding site reduces or abolishes receptor activation. Glycine 63-70 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 102-105 17214961-3 2007 Here, we show that antagonists of and substitutions within the glycine-binding site of NR1 potentiate NR1/NR3 receptor function up to 25-fold, but inhibition or mutation of the NR3 glycine binding site reduces or abolishes receptor activation. Glycine 181-188 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 87-90 17214961-4 2007 Thus, glycine bound to the NR1 subunit causes auto-inhibition of NR1/NR3 receptors whereas glycine binding to the NR3 subunits is required for opening of the ion channel. Glycine 6-13 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 27-30 17214961-4 2007 Thus, glycine bound to the NR1 subunit causes auto-inhibition of NR1/NR3 receptors whereas glycine binding to the NR3 subunits is required for opening of the ion channel. Glycine 6-13 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 65-68 17214961-5 2007 Our results establish differential roles of the high-affinity NR3 and low-affinity NR1 glycine-binding sites in excitatory glycine receptor function. Glycine 87-94 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 83-86 17047094-1 2007 N-Methyl-D-aspartate receptors (NMDARs) composed of NR1 and NR3 subunits differ from other NMDAR subtypes in that they require glycine alone for activation. Glycine 127-134 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 52-55 17047094-6 2007 Ligand studies of NR1/NR3 receptors also suggest differential agonist selectivity between NR3 and NR1, as some high-affinity NR1 agonists only minimally activate NR1/NR3 receptors, whereas other NR1 agonists are as potent as glycine. Glycine 225-232 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 18-21 17047094-6 2007 Ligand studies of NR1/NR3 receptors also suggest differential agonist selectivity between NR3 and NR1, as some high-affinity NR1 agonists only minimally activate NR1/NR3 receptors, whereas other NR1 agonists are as potent as glycine. Glycine 225-232 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 98-101 17047094-6 2007 Ligand studies of NR1/NR3 receptors also suggest differential agonist selectivity between NR3 and NR1, as some high-affinity NR1 agonists only minimally activate NR1/NR3 receptors, whereas other NR1 agonists are as potent as glycine. Glycine 225-232 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 98-101 17047094-6 2007 Ligand studies of NR1/NR3 receptors also suggest differential agonist selectivity between NR3 and NR1, as some high-affinity NR1 agonists only minimally activate NR1/NR3 receptors, whereas other NR1 agonists are as potent as glycine. Glycine 225-232 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 98-101 17047094-6 2007 Ligand studies of NR1/NR3 receptors also suggest differential agonist selectivity between NR3 and NR1, as some high-affinity NR1 agonists only minimally activate NR1/NR3 receptors, whereas other NR1 agonists are as potent as glycine. Glycine 225-232 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 98-101 16417568-6 2006 When co-expressing NR1(stop838)/NR2A the effects of PMA could only be observed with agonist concentrations sufficient to induce glycine-insensitive desensitization. Glycine 128-135 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 19-22 16281028-2 2005 These receptors are heteromeric ion channels that for activation require binding of glycine and glutamate to the NR1 and NR2 subunits, respectively. Glycine 84-91 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 113-116 16281028-4 2005 Here we report crystal structures of the ligand-binding core of NR2A with glutamate and that of the NR1-NR2A heterodimer with glutamate and glycine. Glycine 140-147 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 100-103 15970596-3 2005 Here we report that covalent modification of NR1-A652C or the analogous mutation in NR2A, -2B, -2C, or -2D by methanethiosulfonate ethylammonium (MT-SEA) occurs only in the presence of glutamate and glycine, and that modification potentiates recombinant NMDA receptor currents. Glycine 199-206 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 45-48 16162926-2 2005 They are heteromeric complexes of NR1 combined with NR2A-D and/or NR3A-B subunits that are activated by glutamate and glycine and whose activity is modulated by allosteric modulators. Glycine 118-125 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 34-37 15996549-3 2005 Whereas ACPC and ACBC partially activate the NMDA receptor by 80% and 42%, respectively, their cocrystal structures of the NR1 ligand binding core show the same degree of domain closure as found in the complex with glycine, a full agonist, illustrating that the NR1 subunit provides a new paradigm for partial agonist action that is distinct from that of the evolutionarily related GluR2, AMPA-sensitive receptor. Glycine 215-222 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 123-126 15996549-3 2005 Whereas ACPC and ACBC partially activate the NMDA receptor by 80% and 42%, respectively, their cocrystal structures of the NR1 ligand binding core show the same degree of domain closure as found in the complex with glycine, a full agonist, illustrating that the NR1 subunit provides a new paradigm for partial agonist action that is distinct from that of the evolutionarily related GluR2, AMPA-sensitive receptor. Glycine 215-222 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 262-265 12068077-2 2002 The inhibition constants (K (I) s) for the binding of l-glutamate and glycine to NR1-1a/NR2A determined by [3 H]CGP 39653 and [3 H]MDL 105 519 displacement assays, respectively, were not significantly different between NR1-1a/NR2A receptors coexpressed +/- PSD-95(c-Myc). Glycine 70-77 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 81-84 15650113-6 2005 On the other hand, several residues in the lurcher motif of either NR1 or NR2A are critical for the glycine-independent desensitization of NR1/NR2A receptors. Glycine 100-107 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 67-70 15650113-6 2005 On the other hand, several residues in the lurcher motif of either NR1 or NR2A are critical for the glycine-independent desensitization of NR1/NR2A receptors. Glycine 100-107 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 139-142 15490133-2 2005 Glycine coactivates glutamate N-methyl-D-aspartate (NMDA) receptors by binding to a distinct recognition site on the NR1 subunit. Glycine 0-7 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 117-120 15490133-3 2005 Purely excitatory glycine receptors composed of NR1 and NR3/NR4 NMDA receptor subunits have recently been described, raising the possibility of excitotoxic effects mediated by glycine alone. Glycine 18-25 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 48-51 15597199-5 2004 A short molecular dynamics simulation of the glycine-bound form of wild-type and double-mutated (D481N; K483Q) NR1 subunit structure shows considerable RMSD at the hinge region of S1S2 segment, where pore forming transmembrane helices are located in the native receptor. Glycine 45-52 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 111-114 14722247-4 2004 NR1 binds glycine, and residue Asn598 in the re-entrant membrane loop M2 largely determines NMDAR calcium permeability. Glycine 10-17 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 0-3 14722247-6 2004 Here, we report that mutations of NR1(Asn598) in combination with wild-type NR2A, expressed in human embryonic kidney 293 cells, exhibit altered glycine-independent desensitization. Glycine 145-152 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 34-37 12805203-2 2003 NMDA receptors require both glycine and glutamate for activation with NR1 and NR2 forming glycine and glutamate sites, respectively. Glycine 28-35 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 70-73 12805203-2 2003 NMDA receptors require both glycine and glutamate for activation with NR1 and NR2 forming glycine and glutamate sites, respectively. Glycine 90-97 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 70-73 12805203-4 2003 Here, we describe the cocrystal structures of the NR1 S1S2 ligand-binding core with the agonists glycine and D-serine (DS), the partial agonist D-cycloserine (DCS) and the antagonist 5,7-dichlorokynurenic acid (DCKA). Glycine 97-104 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 50-53 12761330-4 2003 The majority of mutations that strongly affected proton sensitivity were clustered in the extracellular end of the second transmembrane domain (M3) and adjacent linker leading to the S2 portion of the glycine-binding domain of NR1. Glycine 201-208 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 227-230 12068077-1 2002 Coexpression of PSD-95(c-Myc) with NR1-1a/NR2A NMDA receptors in human embryonic kidney (HEK) 293 cells resulted in a decrease in efficacy for the glycine stimulation of [3 H]MK801 binding similar to that previously described for l-glutamate. Glycine 147-154 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 35-38 15650113-0 2005 Molecular determinants of glycine-independent desensitization of NR1/NR2A receptors. Glycine 26-33 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 65-68 15761697-4 2005 RESULTS: Polymorphisms in several genes known to interact with NMDA receptors are related to an altered risk for schizophrenia, and psychotic patients display changes in levels of mRNA encoding NMDA receptors, including the NR1 subunit on which Glycine(B) sites are located. Glycine 245-252 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 224-227 12068077-2 2002 The inhibition constants (K (I) s) for the binding of l-glutamate and glycine to NR1-1a/NR2A determined by [3 H]CGP 39653 and [3 H]MDL 105 519 displacement assays, respectively, were not significantly different between NR1-1a/NR2A receptors coexpressed +/- PSD-95(c-Myc). Glycine 70-77 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 219-222 11754839-3 2001 We have localized regions in the S1 binding domain of both subunits required for the transmission of allosteric signals from the glutamate binding NR2A subunit to the glycine binding NR1 subunit. Glycine 167-174 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 183-186 11572853-9 2001 NR1(F639A) did not alter the agonist potency of glutamate but did produce a leftward shift in the glycine concentration response for receptors containing NR2A and NR2B subunits. Glycine 98-105 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 0-3 11572853-10 2001 NR1(F639A) also reduced the potency of the competitive glycine antagonist 5,7-dichlorokynurenic acid and increased the efficacy of the glycine partial agonist 3-amino-1-hydroxy-2-pyrrolidinone ((+)-HA-966). Glycine 55-62 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 0-3 11572853-10 2001 NR1(F639A) also reduced the potency of the competitive glycine antagonist 5,7-dichlorokynurenic acid and increased the efficacy of the glycine partial agonist 3-amino-1-hydroxy-2-pyrrolidinone ((+)-HA-966). Glycine 135-142 glutamate ionotropic receptor NMDA type subunit 1 Homo sapiens 0-3