Structure of the transmembrane region of the M2 protein H(+) channel

Protein Sci. 2001 Nov;10(11):2241-50. doi: 10.1110/ps.17901.


The transmembrane domain of the M2 protein from influenza A virus forms a nearly uniform and ideal helix in a liquid crystalline bilayer environment. The exposure of the hydrophilic backbone structure is minimized through uniform hydrogen bond geometry imposed by the low dielectric lipid environment. A high-resolution structure of the monomer backbone and a detailed description of its orientation with respect to the bilayer were achieved using orientational restraints from solid-state NMR. With this unique information, the tetrameric structure of this H(+) channel is constrained substantially. Features of numerous published models are discussed in light of the experimental structure of the monomer and derived features of the tetrameric bundle.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Influenza A virus / chemistry*
  • Influenza A virus / pathogenicity
  • Ion Channels / chemistry
  • Magnetic Resonance Spectroscopy / methods
  • Models, Molecular
  • Rotation
  • Viral Matrix Proteins / chemistry*


  • Ion Channels
  • M-protein, influenza virus
  • M2 protein, Influenza A virus
  • Viral Matrix Proteins