5af2
Crystal structure of the C-terminal 2',5'-phosphodiesterase domain of group A rotavirus protein VP3Crystal structure of the C-terminal 2',5'-phosphodiesterase domain of group A rotavirus protein VP3
Structural highlights
Publication Abstract from PubMedIn 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 A 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. This article is protected by copyright. All rights reserved. Crystal structure of the C-terminal 2',5'-phosphodiesterase domain of group A rotavirus protein VP3.,Brandmann T, Jinek M Proteins. 2015 Mar 10. doi: 10.1002/prot.24794. PMID:25758703[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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