Long range allosteric control of cytoplasmic dynein ATPase activity by the stalk and C-terminal domains.

@article{Hk2005LongRA,
  title={Long range allosteric control of cytoplasmic dynein ATPase activity by the stalk and C-terminal domains.},
  author={Peter H{\"o}{\"o}k and Atsushi Mikami and Beth Shafer and Brian T Chait and Steven S. Rosenfeld and Richard B Vallee},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 38},
  pages={
          33045-54
        }
}
The dynein motor domain consists of a ring of six AAA domains with a protruding microtubule-binding stalk and a C-terminal domain of unknown function. To understand how conformational information is communicated within this complex structure, we produced a series of recombinant and proteolytic rat motor domain fragments, which we analyzed enzymatically. A recombinant 210-kDa half-motor domain fragment surprisingly exhibited a 6-fold higher steady state ATPase activity than a 380-kDa complete… CONTINUE READING

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Model for unidirectional movement of axonemal and cytoplasmic dynein molecules.

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  • 2006
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Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosensing at multiple AAA domains.

  • Proceedings of the National Academy of Sciences of the United States of America
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