Journal
FEBS LETTERS
Volume 552, Issue 1, Pages 35-38Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(03)00781-6
Keywords
ion channel; histidine; tryptophan; cation-pi interactions; hydrogen bond; UV Raman spectroscopy
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The M2 protein form influenza A virus forms a tetrameric ion channel, which enables proton passage across biological membranes when the N-terminal side is acidified. Among the amino acid residues in the transmembrane domain of the M2 protein, His37 and Trp41 are essential for the pH-regulated proton conductance. Current knowledge about the structures and interactions of His37 and Trp41 suggests a model for the M2 ion channel, in which the channel is closed by a network of His37 hydrogen bonds at neutral pH and is opened by a His37-Trp41 cation-pi interaction at acidic pH. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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