Structure of TPR Domain–Peptide Complexes Critical Elements in the Assembly of the Hsp70–Hsp90 Multichaperone Machine

@article{Scheufler2000StructureOT,
  title={Structure of TPR Domain–Peptide Complexes Critical Elements in the Assembly of the Hsp70–Hsp90 Multichaperone Machine},
  author={Clemens Scheufler and Achim Brinker and Gleb Bourenkov and Stefano Pegoraro and Luis Moroder and Hans D. Bartunik and F. Ulrich Hartl and Ismail Moarefi},
  journal={Cell},
  year={2000},
  volume={101},
  pages={199-210}
}
The adaptor protein Hop mediates the association of the molecular chaperones Hsp70 and Hsp90. The TPR1 domain of Hop specifically recognizes the C-terminal heptapeptide of Hsp70 while the TPR2A domain binds the C-terminal pentapeptide of Hsp90. Both sequences end with the motif EEVD. The crystal structures of the TPR-peptide complexes show the peptides in an extended conformation, spanning a groove in the TPR domains. Peptide binding is mediated by electrostatic interactions with the EEVD motif… CONTINUE READING
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