Structural Biology Of Factor VIIa/Tissue Factor Initiated Coagulation
| Autor: | Kanagasabai Vadivel, Bajaj Sp |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular Protein Folding Lipoproteins Factor VIIa Article Thromboplastin Tissue factor chemistry.chemical_compound Cations medicine Humans Protein Interaction Domains and Motifs Binding site Blood Coagulation Factor IX Binding Sites Factor VII Factor X Blood Coagulation Factors Coagulation Biochemistry Structural biology chemistry Multiprotein Complexes Biophysics Oxyanion hole medicine.drug |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|