Apo-Hsp90 coexists in two open conformational states in solution.

@article{Bron2008ApoHsp90CI,
  title={Apo-Hsp90 coexists in two open conformational states in solution.},
  author={Patrick Bron and Emmanuel Giudice and Jean-Paul Rolland and Rub{\'e}n M Buey and Pascale Barbier and J Fernando D{\'i}az and Vincent Peyrot and Daniel F Thomas and Cyrille Garnier},
  journal={Biology of the cell},
  year={2008},
  volume={100 7},
  pages={413-25}
}
BACKGROUND INFORMATION Hsp90 (90 kDa heat-shock protein) plays a key role in the folding and activation of many client proteins involved in signal transduction and cell cycle control. The cycle of Hsp90 has been intimately associated with large conformational rearrangements, which are nucleotide-binding-dependent. However, up to now, our understanding of Hsp90 conformational changes derives from structural information, which refers to the crystal states of either recombinant Hsp90 constructs or… CONTINUE READING

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