Phe crystal structure of dimeric kinesin and implications for microtubule-dependent motility
Phe crystal structure of dimeric kinesin and implications for microtubule-dependent motility
复制标题
DOI：
10.1016/s0092-8674(00)80489-4
复制
发表时间：
1997-12-26
期刊：
影响因子：
64.5
通讯作者：
Mandelkow, E
中科院分区：
文献类型：
--
作者：
Kozielski, F;Sack, S;Mandelkow, E
用X-射线晶体学方法研究了大鼠脑驱动蛋白运动区和颈区与ADP结合后的二聚体结构。二聚体的两个头部通过其颈部的卷曲螺旋α-螺旋相互作用连接。它们彼此大致相似;差异最明显的是头颈连接处和颈部螺旋的适度重新取向，以适应卷曲螺旋构象。股骨头显示出关于接近于盘绕线圈的轴的轴的旋转对称性（类似于120度）。这种排列是出乎意料的，因为它与微管晶格不相容。在这种排列中，驱动蛋白二聚体的两个头部不能与微管具有等同的相互作用。
The dimeric form of the kinesin motor and neck domain from rat brain with bound ADP has been solved by X-ray crystallography. The two heads of the dimer are connected via a coiled-coil alpha-helical interaction of their necks. They are broadly similar to one another; differences are most apparent in the head-neck junction and in a moderate reorientation of the neck helices in order to adopt to the coiled-coil conformation. The heads show a rotational symmetry (similar to 120 degrees) about an axis close to that of the coiled-coil. This arrangement is unexpected since it is not compatible with the microtubule lattice. In this arrangement, the two heads of a kinesin dimer could not have equivalent interactions with microtubules.