Sablin E P
Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143, USA.
Curr Opin Cell Biol. 2000 Feb;12(1):35-41. doi: 10.1016/s0955-0674(99)00054-x.
Atomic resolution three-dimensional structures of two oppositely directed kinesin motors - conventional kinesin and non-claret disjunctional (ncd) protein - are now available in their functional dimeric form. A detailed model of the microtubule has also been recently obtained by docking the 3.7 A structure of tubulin into a 20 A map of the microtubule. Recent structural studies of kinesin motors and their microtubule tracks are contributing to our current understanding of kinesin motor mechanisms.
两种方向相反的驱动蛋白——传统驱动蛋白和非红葡萄酒不分离（ncd）蛋白——的原子分辨率三维结构现在以其功能性二聚体形式存在。最近，通过将微管蛋白的3.7埃结构对接至微管的20埃图谱中，也获得了微管的详细模型。驱动蛋白及其微管轨道的最新结构研究有助于我们目前对驱动蛋白运动机制的理解。
