National Institute of Information and Communications Technology, Nishi-ku, Kobe, Japan.
FEBS J. 2011 Sep;278(17):2964-79. doi: 10.1111/j.1742-4658.2011.08253.x. Epub 2011 Aug 8.
Dynein, which is a minus-end-directed microtubule motor, is crucial to a range of cellular processes. The mass of its motor domain is about 10 times that of kinesin, the other microtubule motor. Its large size and the difficulty of expressing and purifying mutants have hampered progress in dynein research. Recently, however, electron microscopy, X-ray crystallography and single-molecule nanometry have shed light on several key unsolved questions concerning how the dynein molecule is organized, what conformational changes in the molecule accompany ATP hydrolysis, and whether two or three motor domains are coordinated in the movements of dynein. This minireview describes our current knowledge of the molecular organization and the force-generating mechanism of dynein, with emphasis on findings from electron microscopy and single-molecule nanometry.
动力蛋白是一种向微管负端运动的马达蛋白，对多种细胞过程至关重要。它的马达结构域的质量大约是另一种微管马达——驱动蛋白的 10 倍。由于其分子尺寸较大，且突变体的表达和纯化困难，因此动力蛋白的研究进展受到了阻碍。然而，最近的电子显微镜、X 射线晶体学和单分子纳米技术研究揭示了一些关于动力蛋白分子结构、分子构象变化伴随 ATP 水解以及两个或三个马达结构域在动力蛋白运动中如何协调的关键问题。这篇综述介绍了我们目前对动力蛋白的分子结构和力产生机制的认识，重点介绍了电子显微镜和单分子纳米技术的研究结果。
