Structural dynamics and multiregion interactions in dynein-dynactin recognition.

@article{Morgan2011StructuralDA,
  title={Structural dynamics and multiregion interactions in dynein-dynactin recognition.},
  author={Jessica L. Morgan and Yujuan Song and Elisar J Barbar},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 45},
  pages={39349-59}
}
Cytoplasmic dynein is a 1.2-MDa multisubunit motor protein complex that, together with its activator dynactin, is responsible for the majority of minus end microtubule-based motility. Dynactin targets dynein to specific cellular locations, links dynein to cargo, and increases dynein processivity. These two macromolecular complexes are connected by a direct interaction between dynactin's largest subunit, p150(Glued), and dynein intermediate chain (IC) subunit. Here, we demonstrate using NMR… CONTINUE READING
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