Structure of the transmembrane region of the M2 protein H+ channel

作者：Junfeng Wang, Sanguk Kim, Frank Kovacs, Timothy A. Cross · 发表于：Protein Science · 年份：2001 · DOI：10.1110/ps.17901 · 被引用次数：237 · 研究领域：Advanced NMR Techniques and Applications、Protein Structure and Dynamics、Lipid Membrane Structure and Behavior

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.