PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Lysine 34-37 serpin family C member 1 Homo sapiens 140-145 10974350-3 2000 The interaction of plasminogen was significantly (>90%) inhibited by lysine, indicating the involvement of kringles in binding antithrombin III. Lysine 72-78 serpin family C member 1 Homo sapiens 130-146 10974350-6 2000 Using carboxypeptidase B digestion, the plasminogen-binding site of antithrombin III was localized to the carboxy-terminus lysine of the anticoagulant protein. Lysine 123-129 serpin family C member 1 Homo sapiens 68-84 10974350-7 2000 Tissue plasminogen activator also interacted with antithrombin III in a time- and concentration-dependent manner and its binding was also significantly (>90%) inhibited by lysine. Lysine 175-181 serpin family C member 1 Homo sapiens 50-66 10850803-7 2000 Substitutions of the lysine at equivalent positions in two other inhibitory serpins, human alpha1-antichymotrypsin and human antithrombin III, also increased stability and decreased inhibitory activity toward alpha-chymotrypsin and thrombin, respectively. Lysine 21-27 serpin family C member 1 Homo sapiens 125-141 10766996-4 2000 The DNA sequencing demonstrated novel mutations in exon 3A of AT3: a G to T substitution at nucleotide position 5333 in codon GAG for Glu 113, causing a stop codon (E113X), and an A to T substitution at position 5338 in codon AAA for Lys 114, forming Asn (K114N). Lysine 234-237 serpin family C member 1 Homo sapiens 62-65 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Lysine 108-114 serpin family C member 1 Homo sapiens 119-131 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Lysine 108-114 serpin family C member 1 Homo sapiens 175-187 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Lysine 108-114 serpin family C member 1 Homo sapiens 175-187 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Lysine 108-114 serpin family C member 1 Homo sapiens 175-187 9692954-11 1998 Homology modeling of PEDF based on the X-ray crystal structures of antithrombin III and ovalbumin shows a region at the center of beta-sheet A-strands 2 and 3- and helix F that has a basic electrostatic surface potential and is densely populated with lysines exposed to the surface (K134, K137, K189, K191, H212, and K214) that are available to interact with various glycosaminoglycans/polyanions. Lysine 251-258 serpin family C member 1 Homo sapiens 67-83 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Lysine 66-69 serpin family C member 1 Homo sapiens 140-145 2229057-4 1990 This amino acid is part of the ATIII region comprising residues 114-154, which contains the highest proportion of basic residues (Arg or Lys), and is known from chemical modification studies to be involved in heparin binding. Lysine 137-140 serpin family C member 1 Homo sapiens 31-36 9065421-0 1997 Lysine residue 114 in human antithrombin III is required for heparin pentasaccharide-mediated activation. Lysine 0-6 serpin family C member 1 Homo sapiens 28-44 9065421-5 1997 In contrast, lysine 114 was found to be critical in the activation of ATIII toward factor Xa. Lysine 13-19 serpin family C member 1 Homo sapiens 70-75 9065421-7 1997 These data are the first to demonstrate a pivotal role for lysine 114 in the pentasaccharide-mediated activation of ATIII. Lysine 59-65 serpin family C member 1 Homo sapiens 116-121 8702852-0 1996 Requirement of lysine residues outside of the proposed pentasaccharide binding region for high affinity heparin binding and activation of human antithrombin III. Lysine 15-21 serpin family C member 1 Homo sapiens 144-160 7947827-0 1994 Lysine-heparin interactions in antithrombin. Lysine 0-6 serpin family C member 1 Homo sapiens 31-43 7947827-2 1994 Lysine residues in two different regions of antithrombin have been proposed to be involved in heparin binding and heparin-mediated acceleration of proteinase inhibition. Lysine 0-6 serpin family C member 1 Homo sapiens 44-56 8910598-0 1996 Role of arginine 132 and lysine 133 in heparin binding to and activation of antithrombin. Lysine 25-31 serpin family C member 1 Homo sapiens 76-88 8288594-2 1994 Point mutations at Arg-180, Arg-245, Lys-248, and Lys-252 in thrombin markedly reduced the efficiency of heparin catalysis by decreasing the stability of the ternary intermediate, whereas the inactivation of thrombin by antithrombin alone was not affected by these mutations. Lysine 50-53 serpin family C member 1 Homo sapiens 220-232 2229057-8 1990 We propose that a cooperation between Lys-125, Arg-129, Lys-136, and Arg-47 exposed at the surface of the inhibitor allows the binding of the essential pentasaccharide domain of heparin which is specific for the ATIII interaction. Lysine 38-41 serpin family C member 1 Homo sapiens 212-217 2229057-8 1990 We propose that a cooperation between Lys-125, Arg-129, Lys-136, and Arg-47 exposed at the surface of the inhibitor allows the binding of the essential pentasaccharide domain of heparin which is specific for the ATIII interaction. Lysine 56-59 serpin family C member 1 Homo sapiens 212-217 2492530-9 1989 Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. Lysine 92-95 serpin family C member 1 Homo sapiens 34-46 2492530-0 1989 Binding of heparin to human antithrombin III activates selective chemical modification at lysine 236. Lysine 90-96 serpin family C member 1 Homo sapiens 28-44 2478364-3 1989 This was characterized by the extent to which a polysaccharide could protect chemical modification of Lys-125 and Lys-136, two lysyl residues of antithrombin which have been implicated in heparin binding. Lysine 102-105 serpin family C member 1 Homo sapiens 145-157 2478364-3 1989 This was characterized by the extent to which a polysaccharide could protect chemical modification of Lys-125 and Lys-136, two lysyl residues of antithrombin which have been implicated in heparin binding. Lysine 114-117 serpin family C member 1 Homo sapiens 145-157 2478364-9 1989 These data clearly demonstrate that the heparin and pentosan polysulfate binding sites of antithrombin overlap (at Lys-125) but are not identical. Lysine 115-118 serpin family C member 1 Homo sapiens 90-102 2492530-9 1989 Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. Lysine 92-95 serpin family C member 1 Homo sapiens 34-46 2492530-1 1989 Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III. Lysine 0-3 serpin family C member 1 Homo sapiens 78-94 2492530-1 1989 Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III. Lysine 9-12 serpin family C member 1 Homo sapiens 78-94 2492530-1 1989 Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III. Lysine 9-12 serpin family C member 1 Homo sapiens 78-94 2492530-2 1989 A new water-soluble color reagent, 4-N,N-dimethylaminoazobenzene-4"-isothiocyano-2"-sulfonic acid (S-DABITC), was used to identify lysine residues of antithrombin III which participate in the binding of heparin. Lysine 131-137 serpin family C member 1 Homo sapiens 150-166 2492530-9 1989 Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. Lysine 83-86 serpin family C member 1 Homo sapiens 34-46 2492530-9 1989 Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. Lysine 92-95 serpin family C member 1 Homo sapiens 34-46 2492530-12 1989 At a heparin/antithrombin molar ratio of 1, the extent of shielding of Lys-125 and Lys-136 and the unmasking of Lys-236 were 25-33%. Lysine 71-74 serpin family C member 1 Homo sapiens 13-25 2492530-12 1989 At a heparin/antithrombin molar ratio of 1, the extent of shielding of Lys-125 and Lys-136 and the unmasking of Lys-236 were 25-33%. Lysine 83-86 serpin family C member 1 Homo sapiens 13-25 2492530-12 1989 At a heparin/antithrombin molar ratio of 1, the extent of shielding of Lys-125 and Lys-136 and the unmasking of Lys-236 were 25-33%. Lysine 83-86 serpin family C member 1 Homo sapiens 13-25 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 17-20 serpin family C member 1 Homo sapiens 101-113 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 17-20 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 17-20 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 101-113 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 101-113 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 101-113 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 145-157 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Lysine 53-59 serpin family C member 1 Homo sapiens 47-52 3121595-7 1987 259, 935-938) have shown that selective chemical modification of a limited number of lysine residues in antithrombin III causes drastic loss of its heparin cofactor activity. Lysine 85-91 serpin family C member 1 Homo sapiens 104-120 3121595-8 1987 We have performed chemical modification of antithrombin III with trinitrobenzene sulfonic acid in order to determine the location of these lysine residues. Lysine 139-145 serpin family C member 1 Homo sapiens 43-59 3110143-2 1987 Modification of antithrombin with limiting amounts of reagent yields an average incorporation of the phosphopyridoxyl label into 1 lysine/protein molecule (Pecon, J. M., and Blackburn, M. N. (1984) J. Biol. Lysine 131-137 serpin family C member 1 Homo sapiens 16-28 3110143-9 1987 This peptide corresponds to a tryptic fragment including residues 115-129 in the sequence of antithrombin, with the modified residue identified as Lys-125. Lysine 147-150 serpin family C member 1 Homo sapiens 93-105 3110143-11 1987 Identification of this critical lysine for heparin binding strongly supports previous data which indicate that the heparin-binding domain of antithrombin is located at the NH2 terminus within one of the disulfide cross-linked loops of the protein. Lysine 32-38 serpin family C member 1 Homo sapiens 141-153 3095926-9 1986 It is concluded that the reaction of aspirin with antithrombin III results in specific acetylation of lysine residues. Lysine 102-108 serpin family C member 1 Homo sapiens 50-66 6462134-7 1981 Heparin must bind to plasmin to accelerate the plasmin-antithrombin III reaction, since the modification of four to five lysine residues of the enzyme inhibits the rate-enhancement effect of heparin and the dissociation of heparin-plasmin complex decreases the inactivation rate of plasmin. Lysine 121-127 serpin family C member 1 Homo sapiens 55-71 849484-3 1977 Thus, the unique specificity for heparin in the anticoagulation system (which involves two or more lysine residues on the antithrombin molecule) is not paralleled by the findings with the basic homopolymers. Lysine 99-105 serpin family C member 1 Homo sapiens 122-134 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Lysine 225-228 serpin family C member 1 Homo sapiens 54-59 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Lysine 236-239 serpin family C member 1 Homo sapiens 54-59 21875153-6 2011 In the protease bound-antithrombin-pentasaccharide complex Lys 114, Pro 12 and Lys 125 form important hydrogen bonding interactions. Lysine 59-62 serpin family C member 1 Homo sapiens 22-34 21875153-6 2011 In the protease bound-antithrombin-pentasaccharide complex Lys 114, Pro 12 and Lys 125 form important hydrogen bonding interactions. Lysine 79-82 serpin family C member 1 Homo sapiens 22-34 6698980-19 1984 These two models can be positioned such that the three lysine residues in the alpha-helix can be matched for maximal interaction with the three sulfate groups in the octasaccharide demonstrated as essential for binding antithrombin III. Lysine 55-61 serpin family C member 1 Homo sapiens 219-235 6420409-0 1984 Pyridoxylation of essential lysines in the heparin-binding site of antithrombin III. Lysine 28-35 serpin family C member 1 Homo sapiens 67-83 6420409-1 1984 Pyridoxal 5"-phosphate was used to selectively modify lysine residues on antithrombin III. Lysine 54-60 serpin family C member 1 Homo sapiens 73-89 6420409-6 1984 To further examine the role of lysine residues in the interaction of antithrombin III with heparin, the protein was singly labeled with pyridoxyl phosphate and affinity fractionated on heparin-agarose. Lysine 31-37 serpin family C member 1 Homo sapiens 69-85 19661062-6 2009 By contrast, mutation of Lys(114) solely affected the preferential interaction of the pentasaccharide with activated antithrombin. Lysine 25-28 serpin family C member 1 Homo sapiens 117-129 19661062-7 2009 These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state. Lysine 165-168 serpin family C member 1 Homo sapiens 124-136 19661062-7 2009 These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state. Lysine 241-244 serpin family C member 1 Homo sapiens 124-136 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Lysine 53-59 serpin family C member 1 Homo sapiens 107-112 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Lysine 53-59 serpin family C member 1 Homo sapiens 107-112 18206177-3 2008 Antithrombin is one of the most important inhibitors of blood coagulation Since its activation by heparin binding requires critical interactions involving 3 Lys residues; we hypothesized that acrolein or homocysteine thiolactone impair antithrombin activity. Lysine 157-160 serpin family C member 1 Homo sapiens 0-12 12556442-5 2003 Kinetic and structural considerations suggest that Phe-122 and Lys-114 act cooperatively through non-ionic interactions to promote P-helix formation and ATIII binding to the pentasaccharide. Lysine 63-66 serpin family C member 1 Homo sapiens 153-158 12161073-3 2002 One residue, Lys 125, is pivotal for antithrombin to recognize and bind the nonreducing-end trisaccharide of the pentasaccharide in an initial low-affinity complex. Lysine 13-16 serpin family C member 1 Homo sapiens 37-49 12369826-5 2002 However, a loss of approximately one ionic interaction on mutation to Arg indicates that the optimal configuration of the network of basic residues of antithrombin that together interact with the pentasaccharide requires a Lys in position 114. Lysine 223-226 serpin family C member 1 Homo sapiens 151-163 12353073-1 2002 Here we report the finding of a new natural antithrombin mutation that confirms the critical contribution of lysine 114 to the binding of the core heparin pentasaccharide, with the replacement of lysine 114 by glutamate causing a complete loss in affinity. Lysine 109-115 serpin family C member 1 Homo sapiens 44-56 12161073-4 2002 Two other residues, Lys 114 and Arg 129, then cooperate with Lys 125 to induce the low-affinity complex into an activated, high-affinity complex, in which a network of electrostatic interactions between antithrombin and the entire pentasaccharide is established. Lysine 20-23 serpin family C member 1 Homo sapiens 203-215 12161073-4 2002 Two other residues, Lys 114 and Arg 129, then cooperate with Lys 125 to induce the low-affinity complex into an activated, high-affinity complex, in which a network of electrostatic interactions between antithrombin and the entire pentasaccharide is established. Lysine 61-64 serpin family C member 1 Homo sapiens 203-215 11741963-4 2002 To investigate the role of helix D elongation in the allosteric activation of antithrombin, we substituted a proline residue for Lys(133). Lysine 129-132 serpin family C member 1 Homo sapiens 78-90 12022882-6 2002 The reactivities of Arg(143) and Lys(147) mutants were improved approximately 2-fold with antithrombin in the absence but not in the presence of heparin cofactors. Lysine 33-36 serpin family C member 1 Homo sapiens 90-102 11939772-0 2002 Importance of lysine 125 for heparin binding and activation of antithrombin. Lysine 14-20 serpin family C member 1 Homo sapiens 63-75 11567021-0 2001 Lysine 114 of antithrombin is of crucial importance for the affinity and kinetics of heparin pentasaccharide binding. Lysine 0-6 serpin family C member 1 Homo sapiens 14-26