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 sars7a

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beta sandwich fold.
Type I integral membrane protein
Not determined.
Not Known

 Introduction - SARS 7a

Sars7a is a type 1 type I integral membrane protein with an N-terminal signal peptide (15 residues), a luminal domain (81 residues), a C-terminal transmembrane helix and a short five-residue tail. The structure of the refolded recombinant soluble domain reveals an Ig-like beta-sandwich fold. Sars7a is expressed on the membrane surface of host cells infected with the virion with the soluble domain exposed outside the cell. Though the structure of the soluble portion of this protein has been determined, its function is still virtually unknown.

 References

Nelson CA, Pekosz A, Lee CA, Diamond MS, Fremont DH. Structure and intracellular targeting of the SARS-coronavirus Orf7a accessory protein. Structure (Camb). 2005 Jan;13(1):75-85.

Chen YY, Shuang B, Tan YX, Meng MJ, Han P, Mo XN, Song QS, Qiu XY, Luo X, Gan QN, Zhang X, Zheng Y, Liu SA, Wang XN, Zhong NS, Ma DL. The protein X4 of severe acute respiratory syndrome-associated coronavirus is expressed on both virus-infected cells and lung tissue of severe acute respiratory syndrome patients and inhibits growth of Balb/c 3T3 cell line. Chin Med J (Engl). 2005 Feb 20;118(4):267-74.  

Fielding BC, Tan YJ, Shuo S, Tan TH, Ooi EE, Lim SG, Hong W, Goh PY. Characterization of a unique group-specific protein (U122) of the severe acute respiratory syndrome coronavirus. J Virol. 2004 Jul;78(14):7311-8.

Pekosz A, Schaecher SR, Diamond MS, Fremont DH, Sims AC, Baric RS. Structure, expression, and intracellular localization of the SARS-CoV accessory proteins 7a and 7b. Adv Exp Med Biol. 2006;581:115-20.

 
 
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