Open AccessCrystallization and preliminary X‐ray crystallographic analysis of blood coagulation factor V‐activating proteinase (RVV‐V) from Russell's viper venom
Author(s) -
Nakayama Daisuke,
Ben Ammar Youssef,
Takeda Soichi
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109046697
Subject(s) - factor x , viper venoms , coagulation , activator (genetics) , chemistry , venom , thrombin , biochemistry , biology , snake venom , immunology , medicine , platelet , receptor
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 Å resolution.