Structural highlights
Function
[YX4_CVHSA] Non-structural protein which is dispensable for virus replication in cell culture.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tan YJ, Fielding BC, Goh PY, Shen S, Tan TH, Lim SG, Hong W. Overexpression of 7a, a protein specifically encoded by the severe acute respiratory syndrome coronavirus, induces apoptosis via a caspase-dependent pathway. J Virol. 2004 Dec;78(24):14043-7. PMID:15564512 doi:http://dx.doi.org/10.1128/JVI.78.24.14043-14047.2004
- ↑ Nelson CA, Pekosz A, Lee CA, Diamond MS, Fremont DH. Structure and intracellular targeting of the SARS-coronavirus Orf7a accessory protein. Structure. 2005 Jan;13(1):75-85. PMID:15642263 doi:http://dx.doi.org/S0969-2126(04)00384-3
