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

@article{Gigant2013StructureOA,
  title={Structure of a kinesin–tubulin complex and implications for kinesin motility},
  author={B. Gigant and W. Wang and B. Dreier and Q. Jiang and Ludovic Pecqueur and A. Pl{\"u}ckthun and C. Wang and Marcel Knossow},
  journal={Nature Structural &Molecular Biology},
  year={2013},
  volume={20},
  pages={1001-1007}
}
  • B. Gigant, W. Wang, +5 authors Marcel Knossow
  • Published 2013
  • Biology, Medicine
  • Nature Structural &Molecular Biology
  • 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… CONTINUE READING
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