Initiation Mechanism of Kinesin's Neck Linker Docking Process

• 来源期刊: 中国物理快报（英文版）
• 关键词: @@
• 年，卷（期）: 2017,（2）
• 页码范围: 117-121
• 页数: 5页
• 语种: 英文
• DOI: 10.1088/0256-307X/34/2/028701

摘要

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 mechanicalanalysis 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.