4wcg: Difference between revisions
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<StructureSection load='4wcg' size='340' side='right'caption='[[4wcg]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='4wcg' size='340' side='right'caption='[[4wcg]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wcg]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4wcg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyprinid_herpesvirus_3 Cyprinid herpesvirus 3] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WCG FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wcg OCA], [https://pdbe.org/4wcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wcg RCSB], [https://www.ebi.ac.uk/pdbsum/4wcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wcg ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A4FTK7_9VIRU A4FTK7_9VIRU] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Cyprinid herpesvirus 3]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Athanasiadis A]] | ||
[[Category: | [[Category: Kus K]] | ||
Revision as of 10:01, 7 April 2023
The binding mode of Cyprinid Herpesvirus3 ORF112-Zalpha to Z-DNAThe binding mode of Cyprinid Herpesvirus3 ORF112-Zalpha to Z-DNA
Structural highlights
FunctionPublication Abstract from PubMedIn vertebrate species the innate immune system down-regulates protein translation in response to viral infection through the action of the dsRNA-activated protein kinase (PKR). In some teleost species another protein kinase, PKZ, plays a similar role but instead of dsRNA binding domains, PKZ has Zalpha domains. These domains recognize the left-handed conformer of dsDNA and dsRNA known as Z-DNA/Z-RNA. Cyprinid herpesvirus 3 (CyHV-3) infects common and koi carp, that have PKZ, and encodes the ORF112 protein that itself bears a Zalpha domain, a putative competitive inhibitor of PKZ. Here we present the crystal structure of ORF112-Zalpha in complex with an 18 bp CpG DNA repeat, at 1.5 A. We demonstrate that the bound DNA is in the left-handed conformation and identify key interactions for the specificity of ORF112. Localization of ORF112 protein in stress granules induced in CyHV-3 infected fish cells suggests a functional behaviour similar to that of Zalpha domains of the interferon-regulated, nucleic acid surveillance proteins ADAR1 and DAI. The Structure of the Cyprinid Herpesvirus 3 ORF112-Zalpha/Z-DNA Complex Reveals a Mechanism of Nucleic Acids Recognition Conserved with E3L, a Poxvirus Inhibitor of Interferon Response.,Kus K, Rakus K, Boutier M, Tsigkri T, Gabriel L, Vanderplasschen A, Athanasiadis A J Biol Chem. 2015 Nov 11. pii: jbc.M115.679407. PMID:26559969[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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