5af2

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5af2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5af2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5af2 RCSB], [http://www.ebi.ac.uk/pdbsum/5af2 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5af2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5af2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5af2 RCSB], [http://www.ebi.ac.uk/pdbsum/5af2 PDBsum]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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 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.
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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<ref>PMID:25758703</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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Revision as of 07:45, 26 March 2015

Crystal structure of the C-terminal 2',5'-phosphodiesterase domain of group A rotavirus protein VP3

5af2, resolution 1.39Å

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