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驱动蛋白-1如何利用核苷酸的能量:驱动蛋白-1单向运动中的构象变化和机械化学耦联。

How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1.

机构信息

College of Education, Shanghai Normal University, Shanghai 200234, China.

School of Science, Hebei University of Technology, Tianjin 300401, China.

出版信息

Int J Mol Sci. 2020 Sep 22;21(18):6977. doi: 10.3390/ijms21186977.

Abstract

Kinesin-1 is a typical motile molecular motor and the founding member of the kinesin family. The most significant feature in the unidirectional motion of kinesin-1 is its processivity. To realize the fast and processive movement on the microtubule lattice, kinesin-1 efficiently transforms the chemical energy of nucleotide binding and hydrolysis to the energy of mechanical movement. The chemical and mechanical cycle of kinesin-1 are coupled to avoid futile nucleotide hydrolysis. In this paper, the research on the mechanical pathway of energy transition and the regulating mechanism of the mechanochemical cycle of kinesin-1 is reviewed.

摘要

驱动蛋白-1 是一种典型的运动分子马达,也是驱动蛋白家族的创始成员。驱动蛋白-1 单向运动的最显著特征是其行进性。为了在微管晶格上实现快速行进性运动,驱动蛋白-1 有效地将核苷酸结合和水解的化学能转化为机械运动的能量。驱动蛋白-1 的化学和机械循环相偶联,以避免无效的核苷酸水解。本文综述了驱动蛋白-1 能量转换的力学途径和机械化学循环调控机制的研究进展。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f530/7555842/b987fd01c444/ijms-21-06977-g001.jpg

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