Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306, United States.
Curr Opin Virol. 2012 Apr;2(2):128-33. doi: 10.1016/j.coviro.2012.01.005. Epub 2012 Feb 16.
The M2 protein from influenza A is a proton channel as a tetramer, with a single transmembrane helix from each monomer lining the pore. Val27 and Trp41 form gates at either end of the pore and His37 mediates the shuttling of protons across a central barrier between the N-terminal and C-terminal aqueous pore regions. Numerous structures of this transmembrane domain and of a longer construct that includes an amphipathic helix are now in the Protein Data Bank. Many structural differences are apparent from samples obtained in a variety of membrane mimetic environments. High-resolution structural results in lipid bilayers have provided novel insights into the functional mechanism of the unique HxxxW cluster in the M2 proton channel.
甲型流感病毒的 M2 蛋白作为四聚体是一种质子通道，每个单体的单一跨膜螺旋构成了孔道。Val27 和 Trp41 形成孔道两端的门，His37 介导质子在 N 端和 C 端水相孔道区域之间的中央屏障的穿梭。目前，该跨膜结构域的许多结构以及包含一个两亲性螺旋的更长结构的结构都已被收入蛋白质数据库。从在各种膜模拟环境中获得的样本中可以明显看出许多结构差异。在脂质双层中的高分辨率结构结果为 M2 质子通道中独特的 HxxxW 簇的功能机制提供了新的见解。
