Human Factor VIII Structure & Function
Technician Amy Griffiths working in the Fay Lab
Factor VIII serves as a protein cofactor for the serine protease, factor IXa in the membrane-dependent conversion of factor X to factor Xa during the blood coagulation cascade reactions. Deficiency or defects in factor VIII result in hemophilia A, the most common of the severe, inherited bleeding disorders. Ongoing studies in our laboratory include physical and biochemical analyses of factor VIII structure, inter-subunit interactions, and intermolecular interactions with other components of the clotting cascade. Overall, our research program is aimed at gaining fundamental insights into the structure, activity and regulation of a protein central to hemostasis. This information will have specific implications for understanding hemophilia A and developing superior therapeutics for its treatment.
- Molecular orientation of Factor VIIIa on the phospholipid membrane surface determined by fluorescence resonance energy transfer. Biochem J. 452, 293-301. (2013 Jun 01).
- Modification of inter-domain interfaces within the A3C1C2 subunit of factor VIII affects its stability and activity. Biochemistry. In press. (2013 May 09).
- Factor VIIIa A2 Subunit Shows a High Affinity Interaction with Factor IXa: Contribution of A2 Subunit Residues 707-714 to the Interaction with Factor IXa. J Biol Chem. In press. (2013 Apr 11).