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Roles of the histidine and tryptophan side chains in the M2 proton channel from influenza A virus
Author(s) -
Takeuchi Hideo,
Okada Atsushi,
Miura Takashi
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00781-6
Subject(s) - side chain , histidine , chemistry , proton , tryptophan , hydrogen bond , ion channel , transmembrane domain , transmembrane protein , amino acid , proton transport , membrane , biophysics , stereochemistry , crystallography , biochemistry , biology , organic chemistry , molecule , physics , receptor , quantum mechanics , polymer
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–π interaction at acidic pH.