1xak
From Proteopedia
STRUCTURE OF THE SARS-CORONAVIRUS ORF7A ACCESSORY PROTEIN
Structural highlights
FunctionNS7A_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.[1] [2] [3] [4] Publication Abstract from PubMedThe 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[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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