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Crystallization and preliminary X-ray crystallographic analysis of blood coagulation factor V-activating proteinase (RVV-V) from Russell's viper venom.

Acta crystallographica. Section F, Structural biology and crystallization communications (2010-01-08)
Daisuke Nakayama, Youssef Ben Ammar, Soichi Takeda
ABSTRACT

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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Factor V Activating Enzyme from Russell's viper venom, lyophilized powder, 20 units/mg protein