Roles of the histidine and tryptophan side chains in the M2 proton channel from influenza A virus

Hideo Takeuchi, Atsushi Okada, Takashi Miura

Research output: Contribution to journalArticlepeer-review

46 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)35-38
Number of pages4
JournalFEBS Letters
Volume552
Issue number1
DOIs
Publication statusPublished - 2003 Sep 18

Keywords

  • Cation-π interaction
  • Histidine
  • Hydrogen bond
  • Ion channel
  • Tryptophan
  • UV Raman spectroscopy

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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