Interaction of kinesin motors, microtubules, and MAPs

被引:36
|
作者
Marx, A.
Mueller, J.
Mandelkow, E. -M.
Hoenger, A.
Mandelkow, E.
机构
[1] Max Planck Unit Struct Mol Biol, D-22607 Hamburg, Germany
[2] European Mol Biol Lab, D-69117 Heidelberg, Germany
关键词
D O I
10.1007/s10974-005-9051-4
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Kinesins are a family of microtubule-dependent motor proteins that carry cargoes such as vesicles, organelles, or protein complexes along microtubules. Here we summarize structural studies of the "conventional" motor protein kinesin-1 and its interactions with microtubules, as determined by X-ray crystallography and cryo-electron microscopy. In particular, we consider the docking between the kinesin motor domain and tubulin subunits and summarize the evidence that kinesin binds mainly to beta tubulin with the switch-2 helix close to the intradimer interface between alpha and beta tubulin.
引用
收藏
页码:125 / 137
页数:13
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