A structural change in the kinesin motor protein that drives motility

Sarah Rice, Abel W. Lin, Daniel Safer, Cynthia L. Hart, Nariman Naber, Bridget O. Carragher, Shane M. Cain, Elena Pechatnikova, Elizabeth M. Wilson-Kubalek, Michael Whittaker, Edward Pate, Roger Cooke, Edwin W. Taylor, Ronald A. Milligan, Ronald D. Vale*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

661 Scopus citations


Kinesin motors power many motile processes by converting ATP energy into unidirectional motion along microtubules. The force-generating and enzymatic properties of conventional kinesin have been extensively studied; however, the structural basis of movement is unknown. Here we have detected and visualized a large conformational change of a ~15-amino-acid region (the neck linker) in kinesin using electron paramagnetic resonance, fluorescence resonance energy transfer, pre-steady state kinetics and cryo-electron microscopy. This region becomes immobilized and extended towards the microtubule 'plus' end when kinesin binds microtubules and ATP, and reverts to a more mobile conformation when γ-phosphate is released after nucleotide hydrolysis. This conformational change explains both the direction of kinesin motion and processive movement by the kinesin dimer.

Original languageEnglish (US)
Pages (from-to)778-784
Number of pages7
Issue number6763
StatePublished - Dec 16 1999

ASJC Scopus subject areas

  • Medicine(all)
  • General


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