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1elr

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Revision as of 18:52, 25 December 2014

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

Structural highlights

1elr is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	1elw
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[STIP1_HUMAN] Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell. 2000 Apr 14;101(2):199-210. PMID:10786835 doi:10.1016/S0092-8674(00)80830-2

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1elr"

@@ Line 8: / Line 8: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1elr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1elr RCSB], [http://www.ebi.ac.uk/pdbsum/1elr PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/STIP1_HUMAN STIP1_HUMAN]] Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1elr

From Proteopedia

Revision as of 18:52, 25 December 2014

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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