View source for 1xak


==STRUCTURE OF THE SARS-CORONAVIRUS ORF7A ACCESSORY PROTEIN==
<StructureSection load='1xak' size='340' side='right'caption='[[1xak]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xak]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome-related_coronavirus Severe acute respiratory syndrome-related coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XAK 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]] 1.8&#8491;</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=1xak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xak OCA], [https://pdbe.org/1xak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xak RCSB], [https://www.ebi.ac.uk/pdbsum/1xak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xak ProSAT], [https://www.topsan.org/Proteins/MCSG/1xak TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NS7A_SARS NS7A_SARS] Plays a role as antagonist of host tetherin (BST2), disrupting its antiviral effect. Acts by binding to BST2 thereby interfering with its glycosylation. May suppress small interfering RNA (siRNA). May bind to host ITGAL, thereby playing a role in attachment or modulation of leukocytes.<ref>PMID:15564512</ref> <ref>PMID:18020948</ref> <ref>PMID:20631126</ref> <ref>PMID:26378163</ref> 
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== Publication Abstract from PubMed ==
The open reading frame (ORF) 7a of the SARS-associated coronavirus (SARS-CoV) encodes a unique type I transmembrane protein of unknown function. We have determined the 1.8 A resolution crystal structure of the N-terminal ectodomain of orf7a, revealing a compact seven-stranded beta sandwich unexpectedly similar in fold and topology to members of the Ig superfamily. We also demonstrate that, in SARS-CoV- infected cells, the orf7a protein is expressed and retained intracellularly. Confocal microscopy studies using orf7a and orf7a/CD4 chimeras implicate the short cytoplasmic tail and transmembrane domain in trafficking of the protein within the endoplasmic reticulum and Golgi network. Taken together, our findings provide a structural and cellular framework in which to explore the role of orf7a in SARS-CoV pathogenesis.

Structure and intracellular targeting of the SARS-coronavirus Orf7a accessory protein.,Nelson CA, Pekosz A, Lee CA, Diamond MS, Fremont DH Structure. 2005 Jan;13(1):75-85. PMID:15642263<ref>PMID:15642263</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Severe acute respiratory syndrome-related coronavirus]]
[[Category: Fremont DH]]
[[Category: Lee CA]]
[[Category: Nelson CA]]