Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/105338
Title: Structural model of the SARS coronavirus E channel in LMPG micelles
Authors: Surya, Wahyu
Li, Yan
Torres, Jaume
Keywords: DRNTU::Science::Biological sciences
Envelope Protein
Solution NMR
Issue Date: 2018
Source: Surya, W., Li, Y., & Torres, J. (2018). Structural model of the SARS coronavirus E channel in LMPG micelles. Biochimica et Biophysica Acta - Biomembranes, 1860(6), 1309-1317. doi:10.1016/j.bbamem.2018.02.017
Series/Report no.: Biochimica et Biophysica Acta - Biomembranes
Abstract: 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 α-helical, and extramembrane intermolecular NOEs suggest interactions that may affect the TM channel conformation.
URI: https://hdl.handle.net/10356/105338
http://hdl.handle.net/10220/48644
ISSN: 0005-2736
DOI: 10.1016/j.bbamem.2018.02.017
Rights: © 2018 Elsevier B.V. All rights reserved. This paper was published in Biochimica et Biophysica Acta - Biomembranes and is made available with permission of Elsevier B.V.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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