This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5x29
From Proteopedia
(Difference between revisions)
| Line 10: | Line 10: | ||
== 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. | ||
| + | |||
| + | 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> | ||
| + | |||
| + | 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
| |||||||||||
Categories: Cvhsa | Li, Y | Surya, W | Torres, J | Envelope protein | Ion channel | Membrane protein | Pentamer | Viral protein
