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dc.contributor.authorKukol, A.
dc.contributor.authorArkin, I.T.
dc.identifier.citationKukol , A & Arkin , I T 2000 , ' Structure of the Influenza C virus CM2 protein transmembrane domain obtained by site-specific infrared dichroism and global molecular dynamics searching ' Journal of Biological Chemistry , vol. 275 , no. 6 , pp. 4225-4229 .
dc.identifier.otherPURE: 420796
dc.identifier.otherPURE UUID: 68e9cfeb-09c3-44e2-8b8d-197a6ec8f175
dc.identifier.otherWOS: 000085288800072
dc.identifier.otherScopus: 0034635424
dc.descriptionFull text of this article is not available in the UHRA
dc.description.abstractThe 115-residue protein CM2 from Influenza C virus has been recently characterized as a tetrameric integral membrane glycoprotein. infrared spectroscopy and site-directed infrared dichroism were utilized here to determine its transmembrane structure. The transmembrane domain of CM2 is cy-helical, and the helices are tilted by beta = (14.6 +/- 3.0)degrees from the membrane normal. The rotational pitch angle about the helix axis omega for the 1-C-13-labeled residues Gly(59) and Leu(66) is omega = (218 +/- 17)degrees, where w is defined as zero for a residue pointing in the direction of the helix tilt. A detailed structure was obtained from a global molecular dynamics search utilizing the orientational data as an energy refinement term. The structure consists of a left-handed coiled-coil with a helix crossing angle of Omega = 16 degrees, The putative transmembrane pore is occluded by the residue Met(65). In addition hydrogen/deuterium exchange experiments show that the core is not accessible to water.en
dc.relation.ispartofJournal of Biological Chemistry
dc.subjectB VIRUS
dc.subjectRNA SEGMENT-6
dc.subjectION CHANNELS
dc.titleStructure of the Influenza C virus CM2 protein transmembrane domain obtained by site-specific infrared dichroism and global molecular dynamics searchingen
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionDepartment of Human and Environmental Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.contributor.institutionAgriculture, Veterinary and Food Sciences
dc.contributor.institutionPharmacology and Clinical Science Research
dc.contributor.institutionCardiovascular Pathologies
dc.contributor.institutionBiochemistry and Bioinformatics
dc.description.statusPeer reviewed
dc.relation.schoolSchool of Life and Medical Sciences
rioxxterms.typeJournal Article/Review

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