کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2048626 | 1074086 | 2011 | 6 صفحه PDF | دانلود رایگان |
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 1.8 Å resolution. The structure reveals multiple interactions between RVV-V and the seven residues, Ile1539 (P7)–Arg1545 (P1), 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.
► We solved the crystal structure of RVV-V in complex with its substrate FV14 peptide.
► We propose a mechanism involved in the factor V recognition for cleavage by RVV-V.
► The narrow specificity of RVV-V is explained.
► First report of the crystal structure of a venom proteinase in complex with its macromolecular substrate.
Journal: FEBS Letters - Volume 585, Issue 19, 3 October 2011, Pages 3020–3025