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Article Dans Une Revue Nature Structural and Molecular Biology Année : 2013

Structure of a kinesin–tubulin complex and implications for kinesin motility

Résumé

The typical function of kinesins is to transport cargo along microtubules. Binding of ATP to microtubule-attached motile kinesins leads to cargo displacement. To better understand the nature of the conformational changes that lead to the power stroke that moves a kinesin's load along a microtubule, we determined the X-ray structure of human kinesin-1 bound to αβ-tubulin. The structure defines the mechanism of microtubule-stimulated ATP hydrolysis, which releases the kinesin motor domain from microtubules. It also reveals the structural linkages that connect the ATP nucleotide to the kinesin neck linker, a 15-amino acid segment C terminal to the catalytic core of the motor domain, to result in the power stroke. ATP binding to the microtubule-bound kinesin favors neck-linker docking. This biases the attachment of kinesin's second head in the direction of the movement, thus initiating each of the steps taken.
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Dates et versions

hal-02121652 , version 1 (06-05-2019)

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Benoît Gigant, Weiyi Wang, Birgit Dreier, Qiyang Jiang, Ludovic Pecqueur, et al.. Structure of a kinesin–tubulin complex and implications for kinesin motility. Nature Structural and Molecular Biology, 2013, 20 (8), pp.1001-1007. ⟨10.1038/nsmb.2624⟩. ⟨hal-02121652⟩

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