Structural biology of factor VIIa/tissue factor initiated coagulation.
Review published in 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.
Resumen
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...
Por qué esto importa para la hirudoterapia
Esta revisión abordó aspectos de biología estructural del complejo factor VIIa/factor tisular, incluyendo el mapeo de los sitios de unión a metales (Ca2+, Mg2+, Na+, Zn2+), las regiones interactivas modeladas de FXa y FIXa con FVIIa/sTF, y el hueco oxianiónico incompletamente formado, con una visión general de los elementos de reconocimiento de TFPI. La relevancia para ASH es mínima: el resumen trata sobre la estructura y función de factores de coagulación pero no involucra sanguijuelas, hirudina ni componentes del secrema de sanguijuela. Advertencia: sin participación de sanguijuelas; relevancia indirecta únicamente como contexto general de bioquímica de la coagulación.
Citación
Structural biology of factor VIIa/tissue factor initiated coagulation.
Vadivel et al. · Frontiers in bioscience (Landmark edition), 2012
Contexto clínico relacionado
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Añadido a la biblioteca ASH: May 28, 2026 · Última actualización del sitio: 18 de junio de 2026