Structural Delineation of the Neck Linker of Kinesin-3 for Processive Movement

J Mol Biol. 2018 Jul 6;430(14):2030-2041. doi: 10.1016/j.jmb.2018.05.010. Epub 2018 May 9.


Processive kinesin motors contain a neck linker (NL) that mediates the chemo-mechanical coupling and controls the directionality and processivity. However, kinesin-3 NL remains poorly determined due to the lack of the structural information of the junction with the following neck coil (NC). Here, we determined the structure of the motor domain (MD)-NL-NCNT tandem of KIF13B that defines the junction between NL and NC and delineates kinesin-3 NL. Unexpectedly, the length of kinesin-3 NL is much shorter than the previously predicted one. In the MD-NL-NCNT structure, NL docks onto the MD with a conventional mode but the interaction between NL and the MD is relatively weak due to the shorter N-terminal cover strand of the MD. The optimal short NL and its weak interaction with the MD would generate the tight inter-head strain and facilitate the NL undocking, which may contribute to the fast and superprocessive motility of kinesin-3.

Keywords: X-ray crystallography; interaction; intracellular transport; molecular dynamics simulation; molecular motor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Humans
  • Kinesins / chemistry*
  • Models, Molecular
  • Molecular Dynamics Simulation
  • Multigene Family
  • Protein Conformation


  • Kinesins