Abstract
AbstractThe 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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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 28, 2002, 6:41 p.m.) |
Deposited | 1 year, 10 months ago (Oct. 8, 2023, 8:24 a.m.) |
Indexed | 1 month ago (July 30, 2025, 10:15 a.m.) |
Issued | 23 years, 10 months ago (Nov. 1, 2001) |
Published | 23 years, 10 months ago (Nov. 1, 2001) |
Published Online | 16 years, 8 months ago (Dec. 31, 2008) |
Published Print | 23 years, 10 months ago (Nov. 1, 2001) |
@article{Wang_2001, title={Structure of the transmembrane region of the M2 protein H+ channel}, volume={10}, ISSN={1469-896X}, url={http://dx.doi.org/10.1110/ps.17901}, DOI={10.1110/ps.17901}, number={11}, journal={Protein Science}, publisher={Wiley}, author={Wang, Junfeng and Kim, Sanguk and Kovacs, Frank and Cross, Timothy A.}, year={2001}, month=nov, pages={2241–2250} }