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.
Structure of the transmembrane region of the M2 protein H(+) channel.,Wang J, Kim S, Kovacs F, Cross TA Protein Sci. 2001 Nov;10(11):2241-50. PMID:11604531[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Wang J, Kim S, Kovacs F, Cross TA. Structure of the transmembrane region of the M2 protein H(+) channel. Protein Sci. 2001 Nov;10(11):2241-50. PMID:11604531
