Domain:domain interactions within Hop, the Hsp70/Hsp90 organizing protein, are required for protein stability and structure.

@article{Carrigan2006DomaindomainIW,
  title={Domain:domain interactions within Hop, the Hsp70/Hsp90 organizing protein, are required for protein stability and structure.},
  author={Patricia E Carrigan and Laura A. Sikkink and David F. Smith and Marina Ram{\'i}rez-Alvarado},
  journal={Protein science : a publication of the Protein Society},
  year={2006},
  volume={15 3},
  pages={522-32}
}
The major heat shock protein (Hsp) chaperones Hsp70 and Hsp90 both bind the co-chaperone Hop (Hsp70/Hsp90 organizing protein), which coordinates Hsp actions in folding protein substrates. Hop contains three tetratricopeptide repeat (TPR) domains that have binding sites for the conserved EEVD C termini of Hsp70 and Hsp90. Crystallographic studies have shown that EEVD interacts with positively charged amino acids in Hop TPR-binding pockets (called carboxylate clamps), and point mutations of these… CONTINUE READING

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