Structural highlights
Function
[NS7A_CVHSA] Non-structural protein which is dispensable for virus replication in cell culture.[1]
Publication Abstract from PubMed
The SARS related Coronavirus genome contains a variety of novel accessory genes. One of these, called ORF7a or ORF8, code for a protein, known as 7a, U122 or X4. We set out to determine the three-dimensional structure of the soluble ectodomain of this type-I transmembrane protein by nuclear magnetic resonance spectroscopy. The fold of the protein is the first member of a further variation of the immunoglobulin like beta-sandwich fold. Because X4 does not reveal significant sequence homologies to proteins in the data bases, we carried out a structure based similarity search for proteins with known function. High structural similarity to Dl domains of ICAM-1 and ICAM-2, and common features in amino acid sequence between X4 and ICAM-1, suggest X4 to possess binding activity for the alpha(L) integrin I domain of LFA-1. Further, based on this structure based prediction, potential functions of X4 in virus replication and pathogenesis are discussed.
Solution structure of the X4 protein coded by the SARS related coronavirus reveals an immunoglobulin like fold and suggests a binding activity to integrin I domains.,Hanel K, Stangler T, Stoldt M, Willbold D J Biomed Sci. 2006 May;13(3):281-93. Epub 2005 Nov 23. PMID:16328780[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
- ↑ Hanel K, Stangler T, Stoldt M, Willbold D. Solution structure of the X4 protein coded by the SARS related coronavirus reveals an immunoglobulin like fold and suggests a binding activity to integrin I domains. J Biomed Sci. 2006 May;13(3):281-93. Epub 2005 Nov 23. PMID:16328780 doi:http://dx.doi.org/10.1007/s11373-005-9043-9
