Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules

Nariman Naber*, Todd J. Minehardt, Sarah Rice, Xiaoru Chen, Jean Grammer, Marija Matuska, Ronald D. Vale, Peter A. Kollman, Roberto Car, Ralph G. Yount, Roger Cooke, Edward Pate

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

50 Scopus citations


We have used adenosine diphosphate analogs containing electron paramagnetic resonance (EPR) spin moieties and EPR spectroscopy to show that the nucleotide-binding site of kinesin-family motors closes when the motor-diphosphate complex binds to microtubules. Structural analyses demonstrate that a domain movement in the switch 1 region at the nucleotide site, homologous to domain movements in the switch 1 region in the G proteins [heterotrimeric guanine nucleotide-binding proteins], explains the EPR data. The switch movement primes the motor both for the free energy-yielding nucleotide hydrolysis reaction and for subsequent conformational changes that are crucial for the generation of force and directed motion along the microtubule.

Original languageEnglish (US)
Pages (from-to)798-801
Number of pages4
Issue number5620
StatePublished - May 2 2003

ASJC Scopus subject areas

  • General


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