2kix

Channel domain of BM2 protein from influenza B virus

spinqualitylabelsall models 2kix Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kix is a 4 chain structure with sequence from Influenza B virus (B/Taiwan/70061/2006). Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B4UQM4_9INFB Publication Abstract from PubMed Influenza B virus contains an integral membrane protein, BM2, that oligomerizes in the viral membrane to form a pH-activated proton channel. Here we report the solution structures of both the membrane-embedded channel domain and the cytoplasmic domain of BM2. The channel domain assumes a left-handed coiled-coil tetramer formation with a helical packing angle of -37 degrees to form a polar pore in the membrane for conducting ions. Mutagenesis and proton flux experiments identified residues involved in proton relay and suggest a mechanism of proton conductance. The cytoplasmic domain of BM2 also forms a coiled-coil tetramer. It has a bipolar charge distribution, in which a negatively charged region interacts specifically with the M1 matrix protein that is involved in packaging the genome in the virion. This interaction suggests BM2 also recruits matrix proteins to the cell surface during virus budding, making BM2 an unusual membrane protein with the dual roles of conducting ions and recruiting proteins to the membrane. Solution structure and functional analysis of the influenza B proton channel.,Wang J, Pielak RM, McClintock MA, Chou JJ Nat Struct Mol Biol. 2009 Dec;16(12):1267-71. Epub 2009 Nov 8. PMID:19898475 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also M2 protein

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