Chowdhury Saikat, Ketcham Stephanie A, Schroer Trina A, Lander Gabriel C
Department of Integrative Structural and Computational Biology, Scripps Research Institute, La Jolla, California, USA.
Department of Biology, Johns Hopkins University, Baltimore, Maryland, USA.
Nat Struct Mol Biol. 2015 Apr;22(4):345-7. doi: 10.1038/nsmb.2996. Epub 2015 Mar 9.
Cytoplasmic dynein associates with dynactin to drive cargo movement on microtubules, but the structure of the dynein-dynactin complex is unknown. Using electron microscopy, we determined the organization of native bovine dynein, dynactin and the dynein-dynactin-microtubule quaternary complex. In the microtubule-bound complex, the dynein motor domains are positioned for processive unidirectional movement, and the cargo-binding domains of both dynein and dynactin are accessible.
胞质动力蛋白与动力蛋白激活蛋白结合，以驱动货物在微管上移动，但动力蛋白-动力蛋白激活蛋白复合物的结构尚不清楚。我们利用电子显微镜确定了天然牛动力蛋白、动力蛋白激活蛋白以及动力蛋白-动力蛋白激活蛋白-微管四级复合物的结构。在与微管结合的复合物中，动力蛋白的马达结构域处于进行性单向移动的位置，动力蛋白和动力蛋白激活蛋白的货物结合结构域都是可及的。
