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Article

Characterization of a thrombomodulin binding site on protein C and its comparison to an activated protein C binding site for factor Va.

Proteins - 15 Feb 2004

Gale Andrew J, Griffin John H

Abstract excerpt

Activation of the anticoagulant human plasma serine protease zymogen, protein C, by a complex of thrombin and the membrane protein, thrombomodulin, generates activated protein C, a physiologic anti-thrombotic, anti-inflammatory and anti-apoptotic agent. Alanine-scanning site-directed mutagenesis of residues in five surface loops of an extensive basic surface on protein C was used to identify residues that play...

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Identifiers

PMID: 14747992
DOI: 10.1002/prot.10627

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

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Characterization of a thrombomodulin binding site on protein C and its comparison to an activated protein C binding site for factor Va.PMID 14747992Read ↗

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The structure-function relationship of activated protein C. Lessons from natural and engineered mutations.Semantic proximity Read ↗

Calcium inhibition of the activation of protein C by thrombin. Role of the P3 and P3' residues.Semantic proximity Read ↗

Molecular characterization of an extended binding site for coagulation factor Va in the positive exosite of activated protein C.Semantic proximity Read ↗

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The affinity of protein C for the thrombin.thrombomodulin complex is determined in a primary way by active site-dependent interactions.Semantic proximity Read ↗

Identification of surface epitopes of human coagulation factor Va that are important for interaction with activated protein C and heparin.Semantic proximity Read ↗

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