Pub. Date : 2015 Apr
PMID : 25659913
11 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | 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 | glutamate ionotropic receptor NMDA type subunit 1 | Homo sapiens |
| 2 | 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 | glutamate ionotropic receptor NMDA type subunit 1 | Homo sapiens |
| 3 | 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 | glutamate ionotropic receptor NMDA type subunit 1 | Homo sapiens |
| 4 | 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 | glutamate ionotropic receptor NMDA type subunit 1 | Homo sapiens |
| 5 | 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 | glutamate ionotropic receptor NMDA type subunit 1 | Homo sapiens |
| 6 | 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 | glutamate ionotropic receptor NMDA type subunit 1 | Homo sapiens |
| 7 | 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 | glutamate ionotropic receptor NMDA type subunit 1 | Homo sapiens |
| 8 | 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 | glutamate ionotropic receptor NMDA type subunit 1 | Homo sapiens |
| 9 | 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 | glutamate ionotropic receptor NMDA type subunit 1 | Homo sapiens |
| 10 | 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 | glutamate ionotropic receptor NMDA type subunit 1 | Homo sapiens |
| 11 | 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 | glutamate ionotropic receptor NMDA type subunit 1 | Homo sapiens |