RVV-V 切割凝血因子 V 的识别结构基础。
Structural basis of coagulation factor V recognition for cleavage by RVV-V.
机构信息
Department of Cardiac Physiology, National Cerebral and Cardiovascular Center Research Institute, Suita, Osaka, Japan.
出版信息
FEBS Lett. 2011 Oct 3;585(19):3020-5. doi: 10.1016/j.febslet.2011.08.022. Epub 2011 Aug 23.
Russell's viper venom factor V (FV) activator (RVV-V) is a thrombin-like proteinase that specifically cleaves the Arg1545-Ser1546 bond of FV. Here we present the crystal structure of RVV-V in complex with the FV14 peptide (residues 1533-1546 of human FV) determined at 1.8Å resolution. The structure reveals multiple interactions between RVV-V and the seven residues, Ile1539 (P(7))-Arg1545 (P(1)), of the cleaved substrate. Comparison with substrate-free structures reveals conformational changes of the RVV-V loops upon substrate binding, suggesting that the multiple interactions are mediated by an induced-fit mechanism. The results provide an explanation for the narrow specificity of RVV-V.
响尾蛇毒因子 V（FV）激活剂（RVV-V）是一种类凝血酶蛋白酶，它特异性地切割 FV 的 Arg1545-Ser1546 键。在这里，我们展示了 RVV-V 与 FV14 肽（人 FV 的残基 1533-1546）复合物的晶体结构，分辨率为 1.8Å。该结构揭示了 RVV-V 与切割底物的七个残基 Ile1539（P(7))-Arg1545（P(1)) 之间的多种相互作用。与无底物结构的比较揭示了底物结合时 RVV-V 环的构象变化，表明这种多种相互作用是通过诱导契合机制介导的。研究结果为 RVV-V 的狭窄特异性提供了解释。
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