Crystallization and preliminary X-ray crystallographic analysis of blood coagulation factor V-activating proteinase (RVV-V) from Russell's viper venom.
Russell's viper venom blood coagulation factor V activator (RVV-V) is a thrombin-like serine proteinase that specifically activates factor V by cleaving a single peptide bond between Arg1545 and Ser1546. Activated factor V combines with activated factor X produced by the enzyme RVV-X in the venom to form the prothombinase complex, which can induce disseminated intravascular coagulopathy in envenomated animals. In the current study, RVV-V was crystallized in order to attempt to understand its substrate specificity for factor V. Four distinct crystal forms of RVV-V were obtained using the sitting-drop vapour-diffusion method and diffraction data sets were collected on SPring-8 beamlines. The best crystal of RVV-V generated data sets to 1.9 A resolution.
Nakayama
Daisuke
D
Department of Cardiac Physiology, National Cardiovascular Center Research Institute, Japan.
Ben Ammar
Youssef
Y
Takeda
Soichi
S
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D005165:Factor V / Q000378:metabolism; D017840:Daboia / Q000378:metabolism; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000378:metabolism; D014757:Viper Venoms / Q000201:enzymology*
D014757:Viper Venoms; D005165:Factor V; D012697:Serine Endopeptidases; C057675:snake venom factor V activator