dc.contributor.authorLi, Yan
dc.contributor.authorSurya, Wahyu
dc.contributor.authorClaudine, Stephanie
dc.contributor.authorTorres, Jaume
dc.identifier.citationLi, 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.en_US
dc.description.abstractCoronavirus 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.en_US
dc.format.extent29 p.en_US
dc.relation.ispartofseriesThe journal of biological chemistryen_US
dc.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].en_US
dc.subjectDRNTU::Science::Biological sciences
dc.titleStructure of a conserved Golgi complex-targeting signal in coronavirus envelope proteinsen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.description.versionAccepted versionen_US

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