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Article

Importance of lysine 125 for heparin binding and activation of antithrombin.

Biochemistry - 16 Apr 2002

Schedin-Weiss Sophia, Desai Umesh R, Bock Susan C, Gettins Peter G W, Olson Steven T, Björk Ingemar

Abstract excerpt

The anticoagulant sulfated polysaccharide, heparin, binds to the plasma coagulation proteinase inhibitor, antithrombin, and activates it by a conformational change that results in a greatly increased rate of inhibition of target proteinases. Lys125 of antithrombin has previously been implicated in this binding by chemical modification and site-directed mutagenesis and by the crystal structure of a complex between...

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Identifiers

PMID: 11939772
DOI: 10.1021/bi012163l

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Importance of lysine 125 for heparin binding and activation of antithrombin.PMID 11939772Read ↗

Heparin-activated antithrombin interacts with the autolysis loop of target coagulation proteases.Semantic proximity Read ↗

The signature 3-O-sulfo group of the anticoagulant heparin sequence is critical for heparin binding to antithrombin but is not required for allosteric activation.Semantic proximity Read ↗

The allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D.Semantic proximity Read ↗

The region of antithrombin interacting with full-length heparin chains outside the high-affinity pentasaccharide sequence extends to Lys136 but not to Lys139.Semantic proximity Read ↗

Residues Tyr253 and Glu255 in strand 3 of beta-sheet C of antithrombin are key determinants of an exosite made accessible by heparin activation to promote rapid inhibition of factors Xa and IXa.Semantic proximity Read ↗

Role of N- and C-terminal amino acids in antithrombin binding to pentasaccharide.Semantic proximity Read ↗

Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease.Semantic proximity Read ↗

Conformational changes in serpins: II. The mechanism of activation of antithrombin by heparin.Semantic proximity Read ↗

Serine 380 (P14) --> glutamate mutation activates antithrombin as an inhibitor of factor Xa.Semantic proximity Read ↗

Glycosaminoglycan contributions to both protein C activation and thrombin inhibition involve a common arginine-rich site in thrombin that includes residues arginine 93, 97, and 101.Semantic proximity Read ↗

Heparin binding affinity of normal and genetically modified antithrombin III measured using a monoclonal antibody to the heparin binding site of antithrombin III.Semantic proximity Read ↗

Amino acid residues in the P6-P'3 region of thrombin-activable fibrinolysis inhibitor (TAFI) do not determine the thrombomodulin dependence of TAFI activation.Semantic proximity Read ↗

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