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

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

Research output: Contribution to journalArticle

210 Citations (Scopus)

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 - Nov 1 2001

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Monomers
Hydrogen
Hydrogen bonds
Proteins
Nuclear magnetic resonance
Crystalline materials
Lipids
Geometry
Liquids
influenza A virus M2 protein

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Structure of the transmembrane region of the M2 protein H+ channel. / Wang, Junfeng; Kim, Sanguk; Kovacs, Frank; Cross, Timothy A.

In: Protein Science, Vol. 10, No. 11, 01.11.2001, p. 2241-2250.

Research output: Contribution to journalArticle

Wang, Junfeng ; Kim, Sanguk ; Kovacs, Frank ; Cross, Timothy A. / Structure of the transmembrane region of the M2 protein H+ channel. In: Protein Science. 2001 ; Vol. 10, No. 11. pp. 2241-2250.
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