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PDBsum entry 1elr
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of tpr domain-Peptide complexes: critical elements in the assembly of the hsp70-Hsp90 multichaperone machine.
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Authors
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C.Scheufler,
A.Brinker,
G.Bourenkov,
S.Pegoraro,
L.Moroder,
H.Bartunik,
F.U.Hartl,
I.Moarefi.
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Ref.
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Cell, 2000,
101,
199-210.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Figure 1. Interaction of the TPR1 Domain of Hop with
Hsc70/Hsp70
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Figure 4.
Figure 4. Schematic Representation of the TPR–Peptide
Interactions
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2000,
101,
199-210)
copyright 2000.
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