Kinesin’s IAK tail domain inhibits initial microtubule-stimulated ADP release

  title={Kinesin’s IAK tail domain inhibits initial microtubule-stimulated ADP release},
  author={David D Hackney and Maryanne F. Stock},
  journal={Nature Cell Biology},
Kinesin undergoes a global folding conformational change from an extended active conformation at high ionic concentrations to a compact inhibited conformation at physiological ionic concentrations. Here we show that much of the observed ATPase activity of folded kinesin is due to contamination with proteolysis fragments that can still fold, but retain an activated ATPase function. In contrast, kinesin that contains an intact IAK-homology region exhibits pronounced inhibition of its ATPase… CONTINUE READING
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Formation of the compact conformer of kinesin requires a C-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity

  • Stock, F M.
  • J. Biol
  • 1999

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