Journal
PROTEIN SCIENCE
Volume 10, Issue 11, Pages 2241-2250Publisher
COLD SPRING HARBOR LAB PRESS
DOI: 10.1110/ps.17901
Keywords
influenza A; membrane protein structure; M2 proton channel; solid-state NMR; PISEMA; PISA wheel; orientational restraints
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Funding
- NIAID NIH HHS [AI 23007, R01 AI023007] Funding Source: Medline
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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.
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