Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties.

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Article

Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties.

The Journal of biological chemistry - 5 Aug 1990

Ehrlich H J, Gebbink R K, Keijer J, Linders M, Preissner K T, Pannekoek H

Abstract excerpt

Serine protease inhibitors ("serpins") are highly homologous proteins which inhibit selected "target" serine proteases by acting as a pseudo-substrate. Their specificity is primarily determined by the amino acid sequence around the carboxyl-terminally located reactive center (P1-P1'). In addition, the association rate constant between a serpin and a serine protease can be dramatically increased by non-protein...

Topics

Amino Acid Sequence
Antithrombin III
Base Sequence
Cloning, Molecular
Escherichia coli
Genetic Vectors
Glycoproteins
Humans
Kinetics
Molecular Sequence Data
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Oligonucleotide Probes

Plasmids

Plasminogen Inactivators

Recombinant Proteins

Serpins

Thrombin

Vitronectin

Source

Open in PubMed

Identifiers

PMID: 1695900

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1695900-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties.PMID 1695900Read ↗

Vitronectin governs the interaction between plasminogen activator inhibitor 1 and tissue-type plasminogen activator.Semantic proximity Read ↗

The structural basis for the pathophysiological relevance of PAI-1 in cardiovascular diseases and the development of potential PAI-1 inhibitorsSemantic proximity Read ↗

The story of the serpin plasminogen activator inhibitor 1: is there any need for another mutant?Semantic proximity Read ↗

Evolution of serpin specificity: cooperative interactions in the reactive-site loop sequence of antithrombin specifically restrict the inhibition of activated protein C.Semantic proximity Read ↗

Thrombin-variable region 1 (VR1). Evidence for the dominant contribution of VR1 of serine proteases to their interaction with plasminogen activator inhibitor 1.Semantic proximity Read ↗

Identification of tissue-type plasminogen activator-specific plasminogen activator inhibitor-1 mutants. Evidence that second sites of interaction contribute to target specificity.Semantic proximity Read ↗

The M358R variant of α(1)-proteinase inhibitor inhibits coagulation factor VIIa.Semantic proximity Read ↗

Three Decades of Research on Plasminogen Activator Inhibitor-1: A Multifaceted SerpinSemantic proximity Read ↗

Structure-function relationships of plasminogen activator inhibitor-1 and its potential as a therapeutic agent.Semantic proximity Read ↗

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

Kinetic characterization of the proteinase binding defect in a reactive site variant of the serpin, antithrombin. Role of the P1' residue in transition-state stabilization of antithrombin-proteinase complex formation.Semantic proximity Read ↗

Construction of a plasminogen activator inhibitor-1 variant without measurable affinity to vitronectin but otherwise normal.Semantic proximity Read ↗

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