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pubmed-article:11604531pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:11604531pubmed:articleTitleStructure of the transmembrane region of the M2 protein H(+) channel.lld:pubmed
pubmed-article:11604531pubmed:affiliationInstitute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32310, USA.lld:pubmed
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