551. Roles of the histidine and tryptophan side chains in the M2 proton channel from influenza A virus
- Author
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Atsushi Okada, Takashi Miura, and Hideo Takeuchi
- Subjects
Models, Molecular ,Stereochemistry ,Protein Conformation ,Ultraviolet Rays ,Biophysics ,Spectrum Analysis, Raman ,Biochemistry ,Viral Matrix Proteins ,Structural Biology ,Cations ,Genetics ,Side chain ,Histidine ,Molecular Biology ,Ion channel ,Ions ,Hydrogen bond ,biology ,Chemistry ,Tryptophan ,Biological membrane ,Hydrogen Bonding ,Cell Biology ,Hydrogen-Ion Concentration ,Cation–π interaction ,Crystallography ,Transmembrane domain ,M2 proton channel ,biology.protein ,UV Raman spectroscopy ,Protons - Abstract
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.
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