Nucleotide-dependent single- to double-headed binding of kinesin

K. Kawaguchi, S. Ishiwata*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    77 Citations (Scopus)


    The motility of kinesin motors is explained by a "hand-over-hand" model in which two heads of kinesin alternately repeat single-headed and double-headed binding with a microtubule. To investigate the binding mode of kinesin at the key nucleotide states during adenosine 5′-triphosphate (ATP) hydrolysis, we measured the mechanical properties of a single kinesin-microtubule complex by applying an external load with optical tweezers. Both the unbinding force and the elastic modulus in solutions containing AMP-PNP (an ATP analog) were twice the value of those in nucleotide-free solution or in the presence of both AMP-PNP and adenosine 5′-diphosphate. Thus, kinesin binds through two heads in the former and one head in the latter two states, which supports a major prediction of the hand-over-hand model.

    Original languageEnglish
    Pages (from-to)667-669
    Number of pages3
    Issue number5504
    Publication statusPublished - 2001 Jan 26

    ASJC Scopus subject areas

    • General


    Dive into the research topics of 'Nucleotide-dependent single- to double-headed binding of kinesin'. Together they form a unique fingerprint.

    Cite this