CRYSTAL STRUCTURE OF FACTOR VAi AND METHOD FOR IDENTIFYING BLOOD FACTOR Va MODULATORS

摘要

The present invention shows the crystal structure of protein C inactivated factor Va (A1.A3.-C1-­C2) that depicts a novel domain arrangement. The newly disclosed orientation has implications for binding to membranes essential for function. A high-affinity calcium binding site and a copper binding site have been identified, neither of which show a direct involvement in chain association. This structure represents the largest physiologically relevant fragment of factor Va solved to date and provides a new scaffold for generation of models of coagulation factors.