Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/79405
Title: Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins
Authors: Li, Yan
Surya, Wahyu
Claudine, Stephanie
Torres, Jaume
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2014
Source: Li, Y., Surya, W., Claudine, S., & Torres, J. (2014). Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins. The journal of biological chemistry, 289(18), 12535-12549.
Series/Report no.: The journal of biological chemistry
Abstract: Coronavirus envelope (CoV E) proteins are ∼100-residue polypeptides with at least one channel-forming α-helical transmembrane (TM) domain. The extramembrane C-terminal tail contains a completely conserved proline, at the center of a predicted β-coil-β 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 β-coil-β motif forms a short membrane-bound α-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.
URI: https://hdl.handle.net/10356/79405
http://hdl.handle.net/10220/25655
DOI: 10.1074/jbc.M114.560094
Schools: School of Biological Sciences 
Rights: © 2014 The American Society for Biochemistry and Molecular Biology. This is the author created version of a work that has been peer reviewed and accepted for publication by The Journal of Biological Chemistry, The American Society for Biochemistry and Molecular Biology. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1074/jbc.M114.560094].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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