Crystal structure of the C-terminal 2',5'-phosphodiesterase domain of group A rotavirus protein VP3.
Crystal structure of the C-terminal 2',5'-phosphodiesterase domain of group A rotavirus protein VP3.
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作者：
Brandmann T;Jinek M
哺乳动物的先天免疫系统在病毒感染时诱导产生第二信使2 - 5寡腺苷酸（2-5A），激活潜伏核糖核酸酶L（RNase L），限制病毒复制并促进细胞凋亡。轮状病毒和冠状病毒的一个子集编码水解2-5A的2′，5 ′-磷酸二酯酶，从而抑制RNA酶L活化。我们报告了A组轮状病毒蛋白VP 3的2′，5 ′-磷酸二酯酶结构域的晶体结构，分辨率为1.39 nm。该结构表现出2 H磷酸酯酶折叠，并揭示了保守的活性位点残基，提供了深入了解2-5A降解病毒逃避宿主先天免疫的机制。Proteins 2015; 83：997-1002.© 2015 Wiley Periodicals，Inc.
In response to viral infections, the mammalian innate immune system induces the production of the second messenger 2′–5′ oligoadenylate (2–5A) to activate latent ribonuclease L (RNase L) that restricts viral replication and promotes apoptosis. A subset of rotaviruses and coronaviruses encode 2′,5′‐phosphodiesterase enzymes that hydrolyze 2–5A, thereby inhibiting RNase L activation. We report the crystal structure of the 2′,5′‐phosphodiesterase domain of group A rotavirus protein VP3 at 1.39 Å resolution. The structure exhibits a 2H phosphoesterase fold and reveals conserved active site residues, providing insights into the mechanism of 2–5A degradation in viral evasion of host innate immunity. Proteins 2015; 83:997–1002. © 2015 Wiley Periodicals, Inc.