Structural links to kinesin directionality and movement

被引:29
作者
Wade, RH
Kozielski, F
机构
[1] CEA, Inst Biol Struct, F-38027 Grenoble 1, France
[2] CNRS, F-38027 Grenoble 1, France
来源
NATURE STRUCTURAL BIOLOGY | 2000年 / 7卷 / 06期
关键词
D O I
10.1038/75850
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The kinesin motor proteins generate directional movement along microtubules and are involved in many vital processes, including cell division, in eukaryotes, The kinesin superfamily is characterized by a conserved motor domain of similar to 320 residues. Dimeric constructs of N and C class kinesins, with the motor domains at opposite ends of the heavy chain, move towards microtubule plus and minus ends, respectively. Their crystal structures differ mainly in the region linking the motor domain core to the a-helical coiled coil dimerization domain. Chimeric kinesins show that regions outside of the motor domain core determine the direction of movement and mutations in the linker region have a strong effect on motility, Recent work on chimeras and mutants is discussed in a structural context giving insights to possible molecular mechanisms of kinesin directionality and motility.
引用
收藏
页码:456 / 460
页数:5
相关论文
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