A structural analysis of the AAA+ domains in Saccharomyces cerevisiae cytoplasmic dynein

@article{Gleave2014ASA,
  title={A structural analysis of the AAA+ domains in Saccharomyces cerevisiae cytoplasmic dynein},
  author={E. Gleave and H. Schmidt and A. Carter},
  journal={Journal of Structural Biology},
  year={2014},
  volume={186},
  pages={367 - 375}
}
  • E. Gleave, H. Schmidt, A. Carter
  • Published 2014
  • Biology, Medicine
  • Journal of Structural Biology
  • Dyneins are large protein complexes that act as microtubule based molecular motors. The dynein heavy chain contains a motor domain which is a member of the AAA+ protein family (ATPases Associated with diverse cellular Activities). Proteins of the AAA+ family show a diverse range of functionalities, but share a related core AAA+ domain, which often assembles into hexameric rings. Dynein is unusual because it has all six AAA+ domains linked together, in one long polypeptide. The dynein motor… CONTINUE READING
    16 Citations
    Review: Structure and mechanism of the dynein motor ATPase
    • 57
    Dynein motors: How AAA+ ring opening and closing coordinates microtubule binding and linker movement
    • H. Schmidt
    • Biology, Medicine
    • BioEssays : news and reviews in molecular, cellular and developmental biology
    • 2015
    • 25
    Mechanisms of Regulation of Cytoplasmic Dynein
    Lis1 Has Two Opposing Modes of Regulating Cytoplasmic Dynein
    • 51
    • PDF
    Lis1 has two opposing modes of regulating cytoplasmic dynein
    • PDF
    Structural Basis of ATP Hydrolysis and Intersubunit Signaling in the AAA+ ATPase p97.
    • 42
    A physical model describing the transport mechanisms of cytoplasmic dynein
    • PDF
    AAA+ ATPases: structural insertions under the magnifying glass.

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