Research

We are interested in coagulation factors, von Willebrand factor (vWF), and Factor VIII. Recently, we succeeded in purifying vWF-cleaving protease, which plays an important role in modulation of the vWF multimer size. vWF-cleaving protease is a new member of the ADAMTS metalloprotease family, and we are studying the catalytic mechanism of this protease in collaboration with Dominic Chung. We are also investigating structure/function relationships in Factor VIII. We have expressed the C2 domain of Factor VIII in yeast and are studying the ability of this domain to bind phospholipid vesicles and vWF. These studies are greatly facilited by the crystal structure of the C2 domain, as determined by Barry Stoddard and colleagues.