A Low Affinity Ground State Conformation for the Dynein Microtubule Binding Domain

Dynein interacts with microtubules through a dedicated binding domain that is dynamically controlled to achieve high or low affinity, depending on the state of nucleotide bound in a distant catalytic pocket. The active sites for microtubule binding and ATP hydrolysis communicate via conformational c...

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Bibliografiska uppgifter
Huvudupphovsmän: McNaughton, Lynn, Tikhonenko, Irina, Banavali, Nilesh K., LeMaster, David M., Koonce, Michael P.
Materialtyp: Artigo
Språk:Inglês
Publicerad: American Society for Biochemistry and Molecular Biology 2010
Ämnen:
Protein Structure and Folding
Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC2871468/
https://ncbi.nlm.nih.gov/pubmed/20351100
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.083535
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