Structural studies on the co-chaperone Hop and its complexes with Hsp90.

  title={Structural studies on the co-chaperone Hop and its complexes with Hsp90.},
  author={S C Onuoha and Edward Coulstock and J. G{\"u}nter Grossmann and Sophie E. Jackson},
  journal={Journal of molecular biology},
  volume={379 4},
The tetratricopeptide repeat domain (TPR)-containing co-chaperone Hsp-organising protein (Hop) plays a critical role in mediating interactions between Heat Shock Protein (Hsp)70 and Hsp90 as part of the cellular assembly machine. It also modulates the ATPase activity of both Hsp70 and Hsp90, thus facilitating client protein transfer between the two. Despite structural work on the individual domains of Hop, no structure for the full-length protein exists, nor is it clear exactly how Hop… CONTINUE READING


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CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates

D. Svergun, C. Barberato, M. J. Koch
J. Appl. Crystallogr • 1995
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Nature • 2006

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