Johnson K A, Marchese-Ragona S P, Clutter D B, Holzbaur E L, Chilcote T J
Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802.
J Cell Sci Suppl. 1986;5:189-96. doi: 10.1242/jcs.1986.supplement_5.12.
The structure of dynein isolated from several sources follows the pattern first observed with Tetrahymena 22S dynein, which has three globular heads attached by three flexible strands to a root-like base. Recent biochemical data indicate that there is one ATPase site on each dynein head and that all three heads interact with microtubules in an ATP-sensitive manner. Accordingly, images of dynein in situ can be interpreted in terms of a model for crossbridge action where the roots of the bouquet anchor the dynein to the A-tubule and all three heads reach out to interact with the B-tubule in an ATP-dependent reaction to produce a force for sliding.
从多个来源分离出的动力蛋白的结构遵循了最初在四膜虫22S动力蛋白中观察到的模式，该动力蛋白有三个球状头部，通过三条柔性链连接到一个根状基部。最近的生化数据表明，每个动力蛋白头部有一个ATP酶位点，并且所有三个头部都以ATP敏感的方式与微管相互作用。因此，原位动力蛋白的图像可以根据一种横桥作用模型来解释，在该模型中，束状结构的根部将动力蛋白锚定到A微管上，并且所有三个头部伸出以在ATP依赖性反应中与B微管相互作用，从而产生滑动的力。
