View source for 4xq7


==The crystal structure of the OAS-like domain (OLD) of human OASL==
<StructureSection load='4xq7' size='340' side='right'caption='[[4xq7]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4xq7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XQ7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</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=4xq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xq7 OCA], [https://pdbe.org/4xq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xq7 RCSB], [https://www.ebi.ac.uk/pdbsum/4xq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xq7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OASL_HUMAN OASL_HUMAN] Does not have 2'-5'-OAS activity, but can bind double-stranded RNA. Displays antiviral activity against encephalomyocarditis virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral pathway independent of RNase L.<ref>PMID:9826176</ref> <ref>PMID:18931074</ref> <ref>PMID:20074559</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The oligoadenylate synthetase (OAS) enzymes are cytoplasmic dsRNA sensors belonging to the antiviral innate immune system. Upon binding to viral dsRNA, the OAS enzymes synthesize 2'-5' linked oligoadenylates (2-5As) that initiate an RNA decay pathway to impair viral replication. The human OAS-like (OASL) protein, however, does not harbor the catalytic activity required for synthesizing 2-5As and differs from the other human OAS family members by having two C-terminal ubiquitin-like domains. In spite of its lack of enzymatic activity, human OASL possesses antiviral activity. It was recently demonstrated that the ubiquitin-like domains of OASL could substitute for K63-linked poly-ubiquitin and interact with the CARDs of RIG-I and thereby enhance RIG-I signaling. However, the role of the OAS-like domain of OASL remains unclear. Here we present the crystal structure of the OAS-like domain, which shows a striking similarity with activated OAS1. Furthermore, the structure of the OAS-like domain shows that OASL has a dsRNA binding groove. We demonstrate that the OAS-like domain can bind dsRNA and that mutating key residues in the dsRNA binding site is detrimental to the RIG-I signaling enhancement. Hence, binding to dsRNA is an important feature of OASL that is required for enhancing RIG-I signaling.

Structural and functional analysis reveals that human OASL binds dsRNA to enhance RIG-I signaling.,Ibsen MS, Gad HH, Andersen LL, Hornung V, Julkunen I, Sarkar SN, Hartmann R Nucleic Acids Res. 2015 Apr 29. pii: gkv389. PMID:25925578<ref>PMID:25925578</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4xq7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Andersen LL]]
[[Category: Gad HH]]
[[Category: Hartmann R]]
[[Category: Hornung V]]
[[Category: Ibsen MS]]
[[Category: Julkunen I]]
[[Category: Sarkar SN]]