[HTML][HTML] Molecular characterization of an extended binding site for coagulation factor Va in the positive exosite of activated protein C
AJ Gale, A Tsavaler, JH Griffin - Journal of Biological Chemistry, 2002 - ASBMB
The anticoagulant human plasma serine protease, activated protein C (APC), inhibits blood
coagulation by specific inactivation of the coagulation cofactors factor Va (FVa) and factor
VIIIa. Site-directed mutagenesis of residues in three surface loops of a positive exosite
located on APC was used to identify residues that play a significant role in binding to FVa.
Eighteen different residues were mutated to alanine singly, in pairs, or in triple mutation
combinations. Mutant APC proteins were purified and characterized for their inactivation of …
coagulation by specific inactivation of the coagulation cofactors factor Va (FVa) and factor
VIIIa. Site-directed mutagenesis of residues in three surface loops of a positive exosite
located on APC was used to identify residues that play a significant role in binding to FVa.
Eighteen different residues were mutated to alanine singly, in pairs, or in triple mutation
combinations. Mutant APC proteins were purified and characterized for their inactivation of …