Zhong Q, Husslein T, Moore P B, Newns D M, Pattnaik P, Klein M L
Center for Molecular Modeling and Department of Chemistry, University of Pennsylvania, Philadelphia 19104-6323, USA.
FEBS Lett. 1998 Sep 4;434(3):265-71. doi: 10.1016/s0014-5793(98)00988-0.
Molecular dynamics simulations have been performed on a tetramer of the 25-residue (SSDPLVVAASIIGILHLILWILDRL) synthetic peptide [1] which contains the transmembrane domain of the influenza A virus M2 coat protein. The peptide bundle was initially assembled as a parallel alpha-helix bundle in the octane portion of a phase separated water/octane system, which provided a membrane-mimetic environment. A 4-ns dynamics trajectory identified a left-handed coiled coil state of the neutral bundle, with a water filled funnel-like structural motif at the N-terminus involving the long hydrophobic sequence. The neck of the funnel begins at V27 and terminates at H37, which blocks the channel. The C-terminus is held together by inter-helix hydrogen bonds and contains water below H37. Solvation of the S23 and D24 residues, located at the rim of the funnel, appears to be important for stability of the structure. The calculated average tilt of the helices in the neutral bundle is 27 +/- 5 degrees, which agrees well with recent NMR data.
已对包含甲型流感病毒M2衣壳蛋白跨膜结构域的25个残基（SSDPLVVAASIIGILHLILWILDRL）合成肽的四聚体进行了分子动力学模拟[1]。肽束最初在相分离的水/辛烷系统的辛烷部分组装成平行α-螺旋束，该系统提供了类似膜的环境。一条4纳秒的动力学轨迹确定了中性束的左手卷曲螺旋状态，在N端有一个充满水的漏斗状结构基序，涉及长疏水序列。漏斗的颈部从V27开始，在H37处终止，从而阻塞通道。C端通过螺旋间氢键结合在一起，并且在H37下方含有水。位于漏斗边缘的S23和D24残基的溶剂化似乎对结构的稳定性很重要。中性束中螺旋的计算平均倾斜度为27±5度，这与最近的核磁共振数据非常吻合。
