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A molecular motor finds its track

Nature Structural & Molecular Biology volume 20, pages 920–921 (2013)Cite this article

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The detailed mechanism by which the molecular motors kinesin and myosin travel along their respective protein tracks as they generate force during motile processes is still poorly understood. In a recent breakthrough, a crystal structure of kinesin in complex with tubulin illuminates the atomic-level details of a motor-track interaction, answering many questions yet leaving a number of mysteries unresolved.

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Figure 1: Structure of the kinesin-1 motor domain in complex with αβ-tubulin.
Figure 2: Model for the kinesin mechanochemical cycle.

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Authors and Affiliations

  1. Jared C. Cochran is at the Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana, USA.,

    Jared C Cochran

  2. F. Jon Kull is at the Department of Chemistry, Dartmouth College, Hanover, New Hampshire, USA.,

    F Jon Kull

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  1. Jared C Cochran
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  2. F Jon Kull
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Correspondence to F Jon Kull.

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The authors declare no competing financial interests.

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Cochran, J., Kull, F. A molecular motor finds its track. Nat Struct Mol Biol 20, 920–921 (2013). https://doi.org/10.1038/nsmb.2644

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