Amerikanische Gesellschaft für Hirudotherapie

Structural biology of factor VIIa/tissue factor initiated coagulation.

Review published in Frontiers in bioscience (Landmark edition) (2012)

Zuletzt aktualisiert: June 18, 2026Geprüft von: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Narrative reviewArzneimittelentwicklungVadivel et al. · Frontiers in bioscience (Landmark edition), 2012

Abstract

Factor VII (FVII) consists of an N-terminal gamma-carboxyglutamic acid domain followed by two epidermal growth factor-like (EGF1 and EGF2) domains and the C-terminal protease domain. Activation of FVII results in a two-chain FVIIa molecule consisting of a light chain (Gla-EGF1-EGF2 domains) and a heavy chain (protease domain) held together by a single disulfide bond. During coagulation, the complex of tissue factor (TF, a transmembrane glycoprotein) and FVIIa activates factor IX (FIX) and factor X (FX). FVIIa is structurally "zymogen-like" and when bound to TF, it is more "active enzyme-like." FIX and FX share structural homology with FVII. Three structural biology aspects of FVIIa/TF are presented in this review. One, regions in soluble TF (sTF) that interact with FVIIa as well as mapping of Ca2+, Mg2+, Na+ and Zn2+ sites in FVIIa and their functions; two, modeled interactive regions of Gla and EGF1 domains of FXa and FIXa with FVIIa/sTF; and three, incompletely formed oxyanion hole in FVIIa/sTF and its induction by substrate/inhibitor. Finally, an overview of the recognition elements in TF pathway inhibitor is provided.

Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.

Publication typeJournal ArticleReview
Indexed MeSH termsBinding SitesBlood CoagulationBlood Coagulation FactorsCationsFactor VIIaHumansLipoproteinsModels, MolecularMultiprotein ComplexesProtein FoldingProtein Interaction Domains and MotifsThromboplastin

Zusammenfassung

Factor VII (FVII) consists of an N-terminal gamma-carboxyglutamic acid domain followed by two epidermal growth factor-like (EGF1 and EGF2) domains and the C-terminal protease domain. Activation of FVII results in a two-chain FVIIa molecule consisting of a light chain (Gla-EGF1-EGF2 domains) and a...

Warum dies für die Hirudotherapie relevant ist

This review covered structural biology aspects of the factor VIIa/tissue factor complex, including mapping of metal-binding sites (Ca2+, Mg2+, Na+, Zn2+), modeled interactive regions of FXa and FIXa with FVIIa/sTF, and the incompletely formed oxyanion hole, with an overview of TFPI recognition elements. The relevance to ASH is minimal — the abstract addresses coagulation factor structure and function but involves no leeches, hirudin, or leech secretome components. Caveat: no leech involvement; indirect relevance as general coagulation biochemistry background only.

Zitation

Structural biology of factor VIIa/tissue factor initiated coagulation.

Vadivel et al. · Frontiers in bioscience (Landmark edition), 2012

DOI

Verwandter klinischer Kontext

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Drug PipelineDrug DevelopmentDirect Thrombin InhibitorsHirudinAnticoagulation CompoundsHemostasisOtolaryngology

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