Motor proteins of the kinesin superfamily: structure and mechanism.

Motor proteins of the kinesin superfamily: structure and mechanism.
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驱动蛋白超家族的运动蛋白:结构和机制。

DOI:
10.1042/bse0350061
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发表时间:
2000
影响因子:
6.4
通讯作者:
F. Kull
F. Kull
中科院分区:
生物学2区
文献类型:
--
作者:
F. Kull

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驱动蛋白是ATP驱动的微管马达蛋白,产生定向力。驱动蛋白超家族目前包括超过100种含有共同运动域的真核蛋白。运动域的核苷酸结合折叠和活性位点化学也存在于肌动蛋白为基础的运动肌球蛋白中。根据其运动域的位置,驱动蛋白可分为三类:N-末端、C-末端和内部驱动蛋白。传统的驱动蛋白以二聚体的形式运作,以协调的、双手交替的方式沿着微管原丝行走。X-射线晶体结构和EM重建显示负端和正端定向马达中驱动蛋白域的四元排列存在重大差异。驱动蛋白的颈部区域,直接邻近运动域,决定方向性。
Kinesins are ATP-driven microtubule motor proteins that produce directed force. The kinesin superfamily currently encompasses over 100 eukaryotic proteins containing a common motor domain. Both the nucleotide-binding fold and active-site chemistry of the motor domain are also present in the actin-based motor, myosin. Kinesins can be classified into three groups based on the position of their motor domains: N-terminal, C-terminal and internal kinesins. Conventional kinesin operates as a dimer, walking in a co-ordinated, hand-over-hand fashion along a microtubule protofilament. X-ray crystal structures and EM reconstructions show major differences in the quaternary arrangement of kinesin domains in minus-end- and plus-end-directed motors. Kinesin's neck region, directly adjacent to the motor domain, dictates directionality.
DOI: 10.1021/bi9722498
发表时间: 1997-12-23
期刊: BIOCHEMISTRY
影响因子: 2.9
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