1elr: Difference between revisions
New page: left|200px<br /> <applet load="1elr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1elr, resolution 1.90Å" /> '''Crystal structure o... |
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[[Image:1elr.gif|left|200px]]<br /> | [[Image:1elr.gif|left|200px]]<br /><applet load="1elr" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1elr, resolution 1.90Å" /> | caption="1elr, resolution 1.90Å" /> | ||
'''Crystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVD'''<br /> | '''Crystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVD'''<br /> | ||
==Overview== | ==Overview== | ||
The adaptor protein Hop mediates the association of the molecular | 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. | ||
==About this Structure== | ==About this Structure== | ||
1ELR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NI and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1ELR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELR OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Brinker, A.]] | [[Category: Brinker, A.]] | ||
[[Category: Hartl, F | [[Category: Hartl, F U.]] | ||
[[Category: Moarefi, I.]] | [[Category: Moarefi, I.]] | ||
[[Category: Scheufler, C.]] | [[Category: Scheufler, C.]] | ||
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[[Category: tpr-domain]] | [[Category: tpr-domain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:29:05 2008'' | ||
Revision as of 13:29, 21 February 2008
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Crystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVD
OverviewOverview
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.
About this StructureAbout this Structure
1ELR is a Single protein structure of sequence from Homo sapiens with and as ligands. 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
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