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Citation
Kaan, H.Y., Hackney, D.D., Kozielski, F. (2011). The structure of the kinesin-1 motor-tail complex reveals the mechanism of autoinhibition.  Science 333(6044): 883--885.
FlyBase ID
FBrf0214689
Publication Type
Research paper
Abstract

When not transporting cargo, kinesin-1 is autoinhibited by binding of a tail region to the motor domains, but the mechanism of inhibition is unclear. We report the crystal structure of a motor domain dimer in complex with its tail domain at 2.2 angstroms and compare it with a structure of the motor domain alone at 2.7 angstroms. These structures indicate that neither an induced conformational change nor steric blocking is the cause of inhibition. Instead, the tail cross-links the motor domains at a second position, in addition to the coiled coil. This "double lockdown," by cross-linking at two positions, prevents the movement of the motor domains that is needed to undock the neck linker and release adenosine diphosphate. This autoinhibition mechanism could extend to some other kinesins.

PubMed ID
PubMed Central ID
PMC3339660 (PMC) (EuropePMC)
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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Science
    Title
    Science
    Publication Year
    1895-
    ISBN/ISSN
    0036-8075 1095-9203
    Data From Reference
    Genes (1)
    Physical Interactions (2)