Mixed Hsp90–cochaperone complexes are important for the progression of the reaction cycle

@article{Li2011MixedHC,
  title={Mixed Hsp90–cochaperone complexes are important for the progression of the reaction cycle},
  author={Jing Li and Klaus Richter and Johannes Buchner},
  journal={Nature Structural &Molecular Biology},
  year={2011},
  volume={18},
  pages={61-66}
}
The chaperone cycle of heat shock protein-90 (Hsp90) involves progression through defined complexes with different cochaperones. It is still enigmatic how the exchange of cochaperones is regulated. The first cochaperone entering the cycle is the Hsp90 ATPase inhibitor Sti1 (Hop in human), which later is replaced by a prolyl isomerase (PPIase) and p23. We found, unexpectedly, that one Sti1 molecule is sufficient to completely inhibit the ATPase of the Hsp90 dimer. Upon addition of a PPIase… CONTINUE READING
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