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

Int J Mol Sci. 2020 Sep 22;21(18)
Jingyu Qin 1 , Hui Zhang 2 , Yizhao Geng 3 , Qing Ji 3
Jingyu Qin 1 , Hui Zhang 2 , Yizhao Geng 3 , Qing Ji 3

[No authors listed]

Author information
  • 1 College of Education, Shanghai Normal University, Shanghai 200234, China.
  • 2 School of Science, Hebei University of Technology, Tianjin 300401, China.
  • 3 Institute of Biophysics, Hebei University of Technology, Tianjin 300401, China.

摘要


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.

KEYWORDS: Kinesin-1, conformational change, mechanochemical coupling, microtubule, neck linker, nucleotide