与微管结合的动力蛋白-动力蛋白激活蛋白复合物的结构组织。
Structural organization of the dynein-dynactin complex bound to microtubules.
作者信息
Chowdhury Saikat, Ketcham Stephanie A, Schroer Trina A, Lander Gabriel C
机构信息
Department of Integrative Structural and Computational Biology, Scripps Research Institute, La Jolla, California, USA.
Department of Biology, Johns Hopkins University, Baltimore, Maryland, USA.
出版信息
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。
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