X-ray structure of motor and neck domains from rat brain kinesin
X-ray structure of motor and neck domains from rat brain kinesin
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DOI：
10.1021/bi9722498
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发表时间：
1997-12-23
期刊：
影响因子：
2.9
通讯作者：
Mandelkow, E
中科院分区：
文献类型：
--
作者：
Sack, S;M端ller, J;Mandelkow, E
我们有。确定了大鼠驱动蛋白头部和颈部结构域的 X 射线结构。核心运动域的折叠类似于最近报道的人类驱动蛋白的折叠[Kull，F.J，等人。 (1996) Nature 380, 550-554]，该结构的新颖特征包括折叠为 β 链的 N 端区域，以及折叠为两条 β 链加 α 螺旋的 C 端从马达结构域到杆结构域的过渡。该螺旋是驱动蛋白颈部的起点，负责运动复合体的二聚化和力传导。尽管运动域核心的折叠与肌球蛋白域（肌动蛋白依赖性运动）的折叠相似，但驱动蛋白颈部的位置和角度与肌球蛋白柄的位置和角度有很大不同，表明这两种运动具有不同的力传导机制。核心马达的 N 端和 C 端被认为负责马达的方向性 [Case, R. B., et al, (1997) Cell 90, 959-966]，采用连接到结构中央 β 片层的 β 链形式。
We have. determined the X-ray structure of rat kinesin head and neck domains. The folding of the core motor domain resembles that of human kinesin reported recently [Kull, F. J,, et al. (1996) Nature 380, 550-554], Novel features of the structure include the N-terminal region, folded as a beta-strand, and the C-terminal transition from the motor to the rod domain, folded as two beta-strands plus an alpha-helix. This helix is the beginning of kinesin's neck responsible for dimerization of the motor complex and for force transduction. Although the folding of the motor domain core is similar to that of a domain of myosin (an actin-dependent motor), the position and angle of kinesin's neck are very different from those of myosin's stalk, suggesting that the two motors have different mechanisms of force transduction. The N- and C-terminal ends of the core motor, thought to be responsible for the directionality of the motors [Case, R. B., et al, (1997) Cell 90, 959-966], take the form of beta-strands attached to the central beta-sheet of the structure.