Crystal structure of the C‐terminal 2′,5′‐phosphodiesterase domain of group a rotavirus protein VP3 |
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| Authors: | Tobias Brandmann Martin Jinek |
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| Affiliation: | Department of Biochemistry, University of Zurich, Zurich, Switzerland |
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| Abstract: | 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. |
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| Keywords: | phosphodiesterase 2– 5A 2H phosphoesterase RNase L oligoadenylate synthase rotavirus innate immunity immune evasion |
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