Cheng J W, Chen C, Huang T H, Chou S H, Chen S H
Institute of Biomedical Science, National Tsing Hua University, Taiwan, ROC.
Biochim Biophys Acta. 1995 Oct 19;1245(2):227-31. doi: 10.1016/0304-4165(95)00080-u.
The propeptide domain in the precursor forms of blood clotting proteins contains the recognition sequences for gamma-carboxylase. In hemophilia B, several point mutations in this propeptide domain are responsible for the inherited disease. A peptide containing the propeptide sequence of factor IX was synthesized by solid phase methods. Two dimensional 1H-NMR and CD studies indicate that this peptide motif adopts an alpha-helical structure in a 40% trifluoroethanol-containing aqueous solution. The results suggest that the amphipathic alpha-helix within the propeptide domain of factor IX could create a recognition surface for gamma-carboxylase. The influences of mutations and their relationship with the alpha-helical structure are discussed.
