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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 t’,thus the other parts of the NL could dock to the motor domain.How the extra t is formed remains elusive.We investigate the extra t 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 t formation.This extra t formation mechanism provides a clear pathway from ATP binding to NL docking of kinesin.