5x29
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/VEMP_CVHSA 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). | [[http://www.uniprot.org/uniprot/VEMP_CVHSA 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). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Coronaviruses (CoV) cause common colds in humans, but are also responsible for the recent Severe Acute, and Middle East, respiratory syndromes (SARS and MERS, respectively). A promising approach for prevention are live attenuated vaccines (LAVs), some of which target the envelope (E) protein, which is a small membrane protein that forms ion channels. Unfortunately, detailed structural information is still limited for SARS-CoV E, and non-existent for other CoV E proteins. Herein, we report a structural model of a SARS-CoV E construct in LMPG micelles with, for the first time, unequivocal intermolecular NOEs. The model corresponding to the detergent-embedded region is consistent with previously obtained orientational restraints obtained in lipid bilayers and in vivo escape mutants. The C-terminal domain is mostly alpha-helical, and extramembrane intermolecular NOEs suggest interactions that may affect the TM channel conformation. | ||
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| + | Structural model of the SARS coronavirus E channel in LMPG micelles.,Surya W, Li Y, Torres J Biochim Biophys Acta. 2018 Jun;1860(6):1309-1317. doi:, 10.1016/j.bbamem.2018.02.017. Epub 2018 Feb 21. PMID:29474890<ref>PMID:29474890</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5x29" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:35, 4 July 2018
NMR structure of the SARS Coronavirus E protein pentameric ion channel
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Categories: Cvhsa | Li, Y | Surya, W | Torres, J | Envelope protein | Ion channel | Membrane protein | Pentamer | Viral protein
