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

Junfeng Wang, Sanguk Kim, Frank Kovacs, Timothy A. Cross

Research output: Contribution to journalArticlepeer-review

225 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)2241-2250
Number of pages10
JournalProtein Science
Issue number11
StatePublished - 2001
Externally publishedYes


  • Influenza A
  • M2 proton channel
  • Membrane protein structure
  • Orientational restraints
  • PISA wheel
  • Solid-state NMR

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Structure of the transmembrane region of the M2 protein H+ channel'. Together they form a unique fingerprint.

Cite this