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Article

Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant.

Journal of molecular biology - 5 Feb 1999

Zhang E, St Charles R, Tulinsky A

Abstract excerpt

The event that initiates the extrinsic pathway of blood coagulation is the association of coagulation factor VIIa (VIIa) with its cell-bound receptor, tissue factor (TF), exposed to blood circulation following tissue injury and/or vascular damage. The natural inhibitor of the TF.VIIa complex is the first Kunitz domain of tissue factor pathway inhibitor (TFPI-K1). The structure of TF. VIIa reversibly inhibited...

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Source

Identifiers

PMID: 9925787
DOI: 10.1006/jmbi.1998.2452

Genes

TFPI

Provenance

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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Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant.PMID 9925787Read ↗

Tissue factor residues Lys165 and Lys166 are essential for rapid formation of the quaternary complex of tissue factor.VIIa with Xa.tissue factor pathway inhibitor.Semantic proximity Read ↗

Molecular interaction between factor VII and tissue factor.Semantic proximity Read ↗

Tissue factor residues that putatively interact with membrane phospholipids.Semantic proximity Read ↗

Structural biology of tissue factor, the initiator of thrombogenesis in vivo 1Semantic proximity Read ↗

A frequent human coagulation Factor VII mutation (A294V, c152) in loop 140s affects the interaction with activators, tissue factor and substrates.Semantic proximity Read ↗

Engineering of substrate selectivity for tissue factor.factor VIIa complex signaling through protease-activated receptor 2.Semantic proximity Read ↗

Structural and mutational analyses of the molecular interactions between the catalytic domain of factor XIa and the Kunitz protease inhibitor domain of protease nexin 2.Semantic proximity Read ↗

P1 and P2' site mutations convert protease nexin-2 from a factor XIa inhibitor to a plasmin inhibitor.Semantic proximity Read ↗

Molecular Basis of Enhanced Activity in Factor VIIa-Trypsin Variants Conveys Insights into Tissue Factor-mediated Allosteric Regulation of Factor VIIa Activity.Semantic proximity Read ↗

Coagulation factor XII protease domain crystal structure.Semantic proximity Read ↗

Molecular characterisation and three-dimensional structural analysis of mutations in 21 unrelated families with inherited factor VII deficiency.Semantic proximity Read ↗

Structure and function of factor XI.Semantic proximity Read ↗

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