Benz J, Bergner A, Hofmann A, Demange P, Göttig P, Liemann S, Huber R, Voges D
Max-Planck-Institut für Biochemie, Abt. Strukturforschung, Martinsried, Germany.
J Mol Biol. 1996 Aug 2;260(5):638-43. doi: 10.1006/jmbi.1996.0426.
The crystal structure of calcium-free recombinant human annexin VI was solved at a resolution of 3.2 A by using the annexin I model for Patterson search and refined to an R-factor of 19.0%. The molecule consists of two similar halves closely resembling annexin I connected by an alpha-helical segment and arranged perpendicular to each other. The calcium and membrane binding sites assigned by structural homology are therefore not located in the same plane. Analysis of the membrane-bound form of annexin VI by electron microscopy shows the two halves of the molecule coplanar with the membrane, but oriented differently to the crystal structure and suggesting a flexible arrangement. Ion channel activity has been found for annexin VI and the half molecules by electrophysiological experiments.
通过使用膜联蛋白I模型进行帕特森搜索，解析出无钙重组人膜联蛋白VI的晶体结构，分辨率为3.2埃，并将其精修至R因子为19.0%。该分子由两个相似的部分组成，这两个部分通过一个α螺旋片段相连，紧密类似于膜联蛋白I，且相互垂直排列。因此，通过结构同源性确定的钙结合位点和膜结合位点并不在同一平面上。通过电子显微镜对膜联蛋白VI的膜结合形式进行分析表明，该分子的两个部分与膜共平面，但与晶体结构的取向不同，这表明其排列具有灵活性。通过电生理实验发现膜联蛋白VI及其半分子具有离子通道活性。
