The Factor VIIIa C2 Domain (Residues 2228–2240) Interacts with the Factor IXa Gla Domain in the Factor Xase Complex

• Published in: The Journal of biological chemistry Vol. 284; no. 6; pp. 3379 - 3388
• Main Authors: Soeda, Tetsuhiro, Nogami, Keiji, Nishiya, Katsumi, Takeyama, Masahiro, Ogiwara, Kenichi, Sakata, Yoichi, Yoshioka, Akira, Shima, Midori
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 06.02.2009; American Society for Biochemistry and Molecular Biology
• Subjects: Cysteine Endopeptidases - chemistry; Cysteine Endopeptidases - genetics; Cysteine Endopeptidases - metabolism; Enzyme Activation - physiology; Factor IXa - chemistry; Factor IXa - genetics; Factor IXa - metabolism; Factor VIIIa - chemistry; Factor VIIIa - genetics; Factor VIIIa - metabolism; Factor X - chemistry; Factor X - genetics; Factor X - metabolism; Humans; Multienzyme Complexes - chemistry; Multienzyme Complexes - genetics; Multienzyme Complexes - metabolism; Neoplasm Proteins - chemistry; Neoplasm Proteins - genetics; Neoplasm Proteins - metabolism; Phospholipids - chemistry; Phospholipids - genetics; Phospholipids - metabolism; Protein Binding - physiology; Protein Structure, Tertiary - physiology; Surface Plasmon Resonance - methods

Factor VIIIa functions as a cofactor for factor IXa in the phospholipid surface-dependent activation of factor X. Both the C2 domain of factor VIIIa and the Gla domain of factor IXa are involved in phospholipid binding and are required for the activation of factor X. In this study, we have examined...