Structural highlights
Function
[VEMP_CVHSA] Component of the viral envelope that plays a central role in virus morphogenesis and assembly. It is sufficient to form virus-like particles. Seems to be important for creating the membrane curvature needed to acquire the rounded, stable and infectious particle phenotype. Acts as a viroporin, inducing the formation of hydrophilic pores in cellular membranes. Also induces apoptosis (By similarity).
Publication Abstract from PubMed
Coronavirus envelope (CoV E) proteins are approximately 100-residue polypeptides with at least one channel-forming alpha-helical transmembrane (TM) domain. The extramembrane C-terminal tail contains a completely conserved proline, at the center of a predicted beta-coil-beta motif. This hydrophobic motif has been reported to constitute a Golgi-targeting signal or a second TM domain. However, no structural data for this or other extramembrane domains in CoV E proteins is available. Herein, we show that the E protein in the severe acute respiratory syndrome virus has only one TM domain in micelles, whereas the predicted beta-coil-beta motif forms a short membrane-bound alpha-helix connected by a disordered loop to the TM domain. However, complementary results suggest that this motif is potentially poised for conformational change or in dynamic exchange with other conformations.
Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins.,Li Y, Surya W, Claudine S, Torres J J Biol Chem. 2014 May 2;289(18):12535-49. doi: 10.1074/jbc.M114.560094. Epub 2014, Mar 25. PMID:24668816[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li Y, Surya W, Claudine S, Torres J. Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins. J Biol Chem. 2014 May 2;289(18):12535-49. doi: 10.1074/jbc.M114.560094. Epub 2014, Mar 25. PMID:24668816 doi:http://dx.doi.org/10.1074/jbc.M114.560094
