Human coagulation factor Xa prevents oligomerization of anti-coagulant phospholipases A₂

Abstract

Anti-coagulant FXa-binding Viperidae snake venom phospholipases A₂ (sPLA₂) have been identified as specific, exogenous, non-competitive FXa-inhibitors. Detailed knowledge of the sites of interaction of PLA₂ with FXa is essential for understanding the hemostatic process at the molecular level and is important for the development of new anti-coagulant drugs. New insight was obtained by structural and biophysical studies including detailed analysis of the CA-CB-binding interface of crotoxin determined by X-ray crystallography and comparison with the CB-FXa-binding interface determined by molecular docking simulations. In this short review we describe our investigations that contribute to a better understanding of the possible role of PLA₂ oligomerisation in the anti-coagulant effect of PLA₂.

• Anti-coagulant site
• coagulation factor Xa
• PLA₂ oligomerization
• snake venom phospholipases A₂