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

218 Scopus citations

Abstract

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
Volume10
Issue number11
DOIs
StatePublished - 2001

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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