CROSS-DISCIPLINARY PHYSICS AND RELATED AREAS OF SCIENCE AND TECHNOLOGY |
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Initiation Mechanism of Kinesin's Neck Linker Docking Process |
Yi-Zhao Geng1,2, Hui Zhang2, Gang Lyu3, Qing Ji1,2,4** |
1Institute of Biophysics, Hebei University of Technology, Tianjin 300401 2School of Science, Hebei University of Technology, Tianjin 300401 3Mathematical and Physical Science School, North China Electric Power University, Baoding 071003 4State Key Laboratory of Theoretical Physics, Institute of Theoretical Physics, Chinese Academy of Sciences, Beijing 100190
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Cite this article: |
Yi-Zhao Geng, Hui Zhang, Gang Lyu et al 2017 Chin. Phys. Lett. 34 028701 |
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Abstract The neck linker (NL) docking to the motor domain is the key force generation process of a kinesin motor. In the initiation step of NL docking the first three residues (LYS325, THR326 and ILE327 in 2KIN) of the NL must form an 'extra turn', thus the other parts of the NL could dock to the motor domain. How the extra turn is formed remains elusive. We investigate the extra turn formation mechanism using structure-based mechanical analysis via molecular dynamics simulation. We find that the motor head rotation induced by ATP binding first drives ILE327 to move towards a hydrophobic pocket on the motor domain. The driving force, together with the hydrophobic interaction of ILE327 with the hydrophobic pocket, then causes a clockwise rotation of THR326, breaks the locking of LYS325, and finally drives the extra turn formation. This extra turn formation mechanism provides a clear pathway from ATP binding to NL docking of kinesin.
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Received: 07 November 2016
Published: 25 January 2017
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PACS: |
87.16.Nn
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(Motor proteins (myosin, kinesin dynein))
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87.10.Tf
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(Molecular dynamics simulation)
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87.15.hp
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(Conformational changes)
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Fund: Supported by the National Natural Science Foundation of China under Grant Nos 11545014 and 11605038, and the Open Project Program of State Key Laboratory of Theoretical Physics of Institute of Theoretical Physics of Chinese Academy of Science under Grant No Y5KF211CJ1. |
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