1elw: Difference between revisions

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[[Image:1elw.~~gif~~|left|200px]]

[[Image:1elw.png|left|200px]]

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~~'''~~Crystal structure of the TPR1 domain of HOP in complex with a HSC70 peptide~~'''~~

===Crystal structure of the TPR1 domain of HOP in complex with a HSC70 peptide===

~~==Overview==~~

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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.

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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==About this Structure==

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[[Category: Protein binding]]

[[Category: Tpr-domain]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 15~~:15:37 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:57:32 2008''

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-[[Image:1elw.gif|left|200px]]
+{{Seed}}
+[[Image:1elw.png|left|200px]]
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 {{STRUCTURE_1elw|  PDB=1elw  |  SCENE=  }}
-'''Crystal structure of the TPR1 domain of HOP in complex with a HSC70 peptide'''
+===Crystal structure of the TPR1 domain of HOP in complex with a HSC70 peptide===
-==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.
+-->
+{{ABSTRACT_PUBMED_10786835}}
 ==About this Structure==
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 [[Category: Protein binding]]
 [[Category: Tpr-domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:15:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:57:32 2008''