Structure of the transmembrane region of the M2 protein H(+) channel.
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.
Wang
J
J
Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32310, USA.
Kim
S
S
Kovacs
F
F
Cross
T A
TA
D009980:Influenza A virus / Q000737:chemistry* / Q000472:pathogenicity; D007473:Ion Channels / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D012399:Rotation; D014763:Viral Matrix Proteins / Q000737:chemistry*; D000086082:Viroporin Proteins
D007473:Ion Channels; D014763:Viral Matrix Proteins; C031540:M-protein, influenza virus; C488937:M2 protein, Influenza A virus; D000086082:Viroporin Proteins