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1xak
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(New page: 200px<br /><applet load="1xak" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xak, resolution 1.80Å" /> '''STRUCTURE OF THE SAR...)
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Revision as of 03:49, 21 November 2007
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STRUCTURE OF THE SARS-CORONAVIRUS ORF7A ACCESSORY PROTEIN
Overview
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.
About this Structure
1XAK is a Single protein structure of sequence from Human sars coronavirus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 05:56:48 2007
