来自锯鳞蝰蛇毒的凝血因子V激活蛋白酶（RVV-V）的结晶及初步X射线晶体学分析。
Crystallization and preliminary X-ray crystallographic analysis of blood coagulation factor V-activating proteinase (RVV-V) from Russell's viper venom.
作者信息
Nakayama Daisuke, Ben Ammar Youssef, Takeda Soichi
机构信息
Department of Cardiac Physiology, National Cardiovascular Center Research Institute, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt 12):1306-8. doi: 10.1107/S1744309109046697. Epub 2009 Nov 27.
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.
摘要
罗素蝰蛇毒凝血因子V激活剂（RVV-V）是一种类凝血酶丝氨酸蛋白酶，它通过切割精氨酸1545和丝氨酸1546之间的单个肽键来特异性激活因子V。活化的因子V与毒液中酶RVV-X产生的活化因子X结合，形成凝血酶原酶复合物，该复合物可在被蛇毒咬伤的动物中诱发弥散性血管内凝血。在本研究中，为了试图了解其对因子V的底物特异性，对RVV-V进行了结晶。采用坐滴气相扩散法获得了四种不同晶型的RVV-V，并在SPring-8光束线上收集了衍射数据集。RVV-V的最佳晶体产生了分辨率为1.9埃的数据集。
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