The protein structure and effect of factor VIII.

Abstract

Factor VIII (FVIII) is a key component of the fluid phase of the blood coagulation system. The proteases efficiently cleave FVIII at three sites, two within the heavy and one within the light chain resulting in alteration of its covalent structure and conformation and yielding the active cofactor, FVIIIa. FVIIIa is a trimer composed of A1, A2 and A3-C1-C2 subunits. The role of FVIIIa is to markedly increase the catalytic efficiency of factor IXa in the activation of factor X. Variants of these factors frequently also lead to severe bleeding disorders.

• Authors: Hong Fang, Lemin Wang, Hongbao Wang
• Journal: Thrombosis research (Thromb Res) Vol. 119 Issue 1 Pg. 1-13 ( 2007) ISSN: 0049-3848 [Print] United States
• PMID: 16487577 (Publication Type: Journal Article, Review)

Chemical References

• Ions
• Recombinant Proteins
• Factor VIII

Topics

• Blood Coagulation
• Catalytic Domain
• Dimerization
• Factor VIII (chemistry, genetics, physiology)
• Hemophilia A (genetics, metabolism)
• Humans
• Ions
• Mutation
• Protein Binding
• Protein Structure, Tertiary
• Recombinant Proteins (chemistry)