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Article

Arginine 200 of heparin cofactor II promotes intramolecular interactions of the acidic domain. Implication for thrombin inhibition.

The Journal of biological chemistry - 30 May 1997

Ciaccia A V, Monroe D M, Church F C

Abstract excerpt

Heparin cofactor II (HCII) is presumed to be a physiological inhibitor of the serine proteinase thrombin. The reaction between HCII and thrombin is quite unique, because it involves an unusual HCII-reactive site loop sequence of Leu444-Ser445, requires the presence of glycosaminoglycans for optim...

Topics

Arginine
Heparin Cofactor II
Humans
Kinetics
Mutation
Recombinant Proteins
Structure-Activity Relationship
Thrombin

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 9162031
DOI: 10.1074/jbc.272.22.14074

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9162031-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Arginine 200 of heparin cofactor II promotes intramolecular interactions of the acidic domain. Implication for thrombin inhibition.PMID 9162031Read ↗

The N-terminal acidic domain of heparin cofactor II mediates the inhibition of alpha-thrombin in the presence of glycosaminoglycans.Semantic proximity Read ↗

Aspartic acid residues 72 and 75 and tyrosine-sulfate 73 of heparin cofactor II promote intramolecular interactions during glycosaminoglycan binding and thrombin inhibition.Semantic proximity Read ↗

Substitution of arginine for Leu444 in the reactive site of heparin cofactor II enhances the rate of thrombin inhibition.Semantic proximity Read ↗

Contribution of basic residues of the A helix of heparin cofactor II to heparin- or dermatan sulfate-mediated thrombin inhibition.Semantic proximity Read ↗

Molecular mapping of the thrombin-heparin cofactor II complex.Semantic proximity Read ↗

Site-directed mutagenesis of arginine 103 and lysine 185 in the proposed glycosaminoglycan-binding site of heparin cofactor II.Semantic proximity Read ↗

Inhibition of a thrombin anion-binding exosite-2 mutant by the glycosaminoglycan-dependent serpins protein C inhibitor and heparin cofactor II.Semantic proximity Read ↗

Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II.Semantic proximity Read ↗

Amino acid residues of heparin cofactor II required for stimulation of thrombin inhibition by sulphated polyanions.Semantic proximity Read ↗

Altering heparin cofactor II at VAL439 (P6) either impairs inhibition of thrombin or confers elastase resistance.Semantic proximity Read ↗

Fusion of the C-terminal triskaidecapeptide of hirudin variant 3 to alpha1-proteinase inhibitor M358R increases the serpin-mediated rate of thrombin inhibition.Semantic proximity Read ↗

Heparin cofactor II is regulated allosterically and not primarily by template effects. Studies with mutant thrombins and glycosaminoglycans.Semantic proximity Read ↗

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