Publication Abstract from PubMed
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.
Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules.,Naber N, Minehardt TJ, Rice S, Chen X, Grammer J, Matuska M, Vale RD, Kollman PA, Car R, Yount RG, Cooke R, Pate E Science. 2003 May 2;300(5620):798-801. PMID:12730601[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
