1ELR: Crystal Structure Of The Tpr2a Domain Of Hop In Complex With The Hsp90 Peptide Meevd

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, with the C-terminal aspartate acting as a two-carboxylate anchor, and by hydrophobic interactions with residues upstream of EEVD. The hydrophobic contacts with the peptide are critical for specificity. These results explain how TPR domains participate in the ordered assembly of Hsp70-Hsp90 multichaperone complexes.
PDB ID: 1ELRDownload
MMDB ID: 91077
PDB Deposition Date: 2000/3/14
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 1ELR: dimeric; determined by author and by software (PISA)
Molecular Components in 1ELR
Label Count Molecule
Proteins (2 molecules)
Tpr2a-domain of HOP(Gene symbol: STIP1)
Molecule annotation
Hsp90-peptide Meevd
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB