KIF14 binds tightly to microtubules and adopts a rigor-like conformation.

@article{Arora2014KIF14BT,
  title={KIF14 binds tightly to microtubules and adopts a rigor-like conformation.},
  author={Kritica Arora and Lama Talje and A. Asenjo and P. Andersen and Kaleem Atchia and M. Joshi and H. Sosa and J. Allingham and B. Kwok},
  journal={Journal of molecular biology},
  year={2014},
  volume={426 17},
  pages={
          2997-3015
        }
}
  • Kritica Arora, Lama Talje, +6 authors B. Kwok
  • Published 2014
  • Biology, Medicine
  • Journal of molecular biology
  • The mitotic kinesin motor protein KIF14 is essential for cytokinesis during cell division and has been implicated in cerebral development and a variety of human cancers. Here we show that the mouse KIF14 motor domain binds tightly to microtubules and does not display typical nucleotide-dependent changes in this affinity. It also has robust ATPase activity but very slow motility. A crystal structure of the ADP-bound form of the KIF14 motor domain reveals a dramatically opened ATP-binding pocket… CONTINUE READING
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