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1 Department of Chemistry, Florida State University, Tallahassee, Florida 32310, USA
2 Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32310, USA
3 The National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida 32310, USA
Reprint requests to: Dr. Timothy A. Cross, National High Magnetic Field Laboratory, 1800 E. Paul Dirac Drive, Tallahassee, Florida 32310, USA; e-mail: cross{at}magnet.fsu.edu; fax: (850) 644-1366.
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.
Keywords: Influenza A; membrane protein structure; M2 proton channel; solid-state NMR; PISEMA; PISA wheel; orientational restraints
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