1elr: Difference between revisions

Revision as of 00:57, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1elr.png

Template:STRUCTURE 1elr

Crystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVDCrystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVD

Template:ABSTRACT PUBMED 10786835

About this StructureAbout this Structure

1ELR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine., Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I, Cell. 2000 Apr 14;101(2):199-210. PMID:10786835

Page seeded by OCA on Tue Jul 1 00:57:05 2008

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OCA

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-'''Crystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVD'''
+===Crystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVD===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10786835}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10786835 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10786835}}
 ==About this Structure==
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 [[Category: Protein binding]]
 [[Category: Tpr-domain]]
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