1xak
STRUCTURE OF THE SARS-CORONAVIRUS ORF7A ACCESSORY PROTEIN
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OverviewOverview
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 StructureAbout this Structure
1XAK is a Single protein structure of sequence from Human sars coronavirus. Full crystallographic information is available from OCA.
ReferenceReference
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
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