Structure of the Influenza C virus CM2 protein transmembrane domain obtained by site-specific infrared dichroism and global molecular dynamics searching
Structure of the Influenza C virus CM2 protein transmembrane domain obtained by site-specific infrared dichroism and global molecular dynamics searching
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DOI：
10.1074/jbc.275.6.4225
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发表时间：
2000-02-11
影响因子：
4.8
通讯作者：
Arkin, IT
中科院分区：
文献类型：
--
作者：
Kukol, A;Arkin, IT
来自C型流感病毒的115个残基的蛋白质CM 2最近被表征为四聚体整合膜糖蛋白。利用红外光谱和定点红外二色性测定其跨膜结构。CM 2的跨膜结构域是cy-螺旋的，并且螺旋从膜法线倾斜β =（14.6 +/-3.0）度。对于1-C-13标记的残基Gly（59）和Leu（66），绕螺旋轴ω的旋转螺距角为ω =（218 +/-17）度，其中对于指向螺旋倾斜方向的残基，w定义为零。一个详细的结构，从全球分子动力学搜索利用的取向数据作为一个能量细化项。该结构由左旋卷曲螺旋组成，螺旋交叉角为Ω = 16度，推定的跨膜孔被残基Met（65）堵塞。此外，氢/氘交换实验表明，核心是不可接近的水。
The 115-residue protein CM2 from Influenza C virus has been recently characterized as a tetrameric integral membrane glycoprotein. infrared spectroscopy and site-directed infrared dichroism were utilized here to determine its transmembrane structure. The transmembrane domain of CM2 is cy-helical, and the helices are tilted by beta = (14.6 +/- 3.0)degrees from the membrane normal. The rotational pitch angle about the helix axis omega for the 1-C-13-labeled residues Gly(59) and Leu(66) is omega = (218 +/- 17)degrees, where w is defined as zero for a residue pointing in the direction of the helix tilt. A detailed structure was obtained from a global molecular dynamics search utilizing the orientational data as an energy refinement term. The structure consists of a left-handed coiled-coil with a helix crossing angle of Omega = 16 degrees, The putative transmembrane pore is occluded by the residue Met(65). In addition hydrogen/deuterium exchange experiments show that the core is not accessible to water.