Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.

@article{Meyer2004StructuralBF,
  title={Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.},
  author={Philippe Meyer and Chrisostomos Prodromou and Chunyan Liao and Bin Hu and S Mark Roe and Cara K. Vaughan and Ignacija Vla{\vs}i{\'c} and Barry Panaretou and Peter W Piper and Laurence H. Pearl},
  journal={The EMBO journal},
  year={2004},
  volume={23 6},
  pages={1402-10}
}
Hsp90 is a molecular chaperone essential for the activation and assembly of many key eukaryotic signalling and regulatory proteins. Hsp90 is assisted and regulated by co-chaperones that participate in an ordered series of dynamic multiprotein complexes, linked to Hsp90 conformationally coupled ATPase cycle. The co-chaperones Aha1 and Hch1 bind to Hsp90 and stimulate its ATPase activity. Biochemical analysis shows that this activity is dependent on the N-terminal domain of Aha1, which interacts… CONTINUE READING
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