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Article

Calcium inhibition of the activation of protein C by thrombin. Role of the P3 and P3' residues.

European journal of biochemistry - 15 Jul 1994

Rezaie A R, Esmon C T

Abstract excerpt

Protein C, a precursor to a natural plasma anticoagulant, and the platelet thrombin receptor, involved in cell activation, both require proteolytic cleavage to be activated. In humans, the sequences adjacent to the scissile bond of protein C, DPR/LID and the thrombin receptor DPR/SFL are similar. Previous studies with Asp-->Gly mutants indicated that both the P3 and the P3' Asp residues make either peptides or...

Topics

Asparagine
Base Sequence
Calcium
Electrophoresis, Polyacrylamide Gel
Glycine
Humans
Molecular Sequence Data
Mutation
Protein C
Receptors, Thrombin
Recombinant Proteins
Thrombin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Thrombomodulin

Source

Identifiers

PMID: 8055928
DOI: 10.1111/j.1432-1033.1994.tb19027.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8055928-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Calcium inhibition of the activation of protein C by thrombin. Role of the P3 and P3' residues.PMID 8055928Read ↗

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

The functional significance of the autolysis loop in protein C and activated protein C.Semantic proximity Read ↗

Role of the activation peptide in the mechanism of protein C activation.Semantic proximity Read ↗

Activation of protein C by the thrombin-thrombomodulin complex: cooperative roles of Arg-35 of thrombin and Arg-67 of protein C.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 ↗

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

Engineering a disulfide bond to stabilize the calcium-binding loop of activated protein C eliminates its anticoagulant but not its protective signaling properties.Semantic proximity Read ↗

Murine thrombin lacks Na+ activation but retains high catalytic activity.Semantic proximity Read ↗

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Met343Val mutation disrupts the shuttling of Trp380 leading to a low-activity conformer of activated protein C and causes thrombosis.Semantic proximity Read ↗

Structural basis for type I and type II deficiencies of antithrombotic plasma protein C: patterns revealed by three-dimensional molecular modelling of mutations of the protease domain.Semantic proximity Read ↗

Trp83 is vital to the interaction with phospholipids in γ-carboxyglutamic acid domain of protein C.Semantic proximity Read ↗

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