University of Hertfordshire

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Original languageEnglish
Pages (from-to)4225-4229
Number of pages5
JournalJournal of Biological Chemistry
Publication statusPublished - 11 Feb 2000


The 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.


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