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[[Image:1elr.gif|left|200px]]


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==Crystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVD==
The line below this paragraph, containing "STRUCTURE_1elr", creates the "Structure Box" on the page.
<StructureSection load='1elr' size='340' side='right'caption='[[1elr]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1elr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELR FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
{{STRUCTURE_1elr| PDB=1elr |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1elr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elr OCA], [https://pdbe.org/1elr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elr RCSB], [https://www.ebi.ac.uk/pdbsum/1elr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elr ProSAT]</span></td></tr>
</table>
== Function ==
[https://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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/el/1elr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1elr ConSurf].
<div style="clear:both"></div>


'''Crystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVD'''
==See Also==
 
*[[HOP protein|HOP protein]]
 
__TOC__
==Overview==
</StructureSection>
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==
1ELR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELR OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/10786835 10786835]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brinker, A.]]
[[Category: Brinker A]]
[[Category: Hartl, F U.]]
[[Category: Hartl FU]]
[[Category: Moarefi, I.]]
[[Category: Moarefi I]]
[[Category: Scheufler, C.]]
[[Category: Scheufler C]]
[[Category: Helical repeat]]
[[Category: Hop]]
[[Category: Hsp90]]
[[Category: Peptide-complex]]
[[Category: Protein binding]]
[[Category: Tpr-domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:15:13 2008''

Latest revision as of 13:04, 20 March 2024

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

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.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

1elr, resolution 1.90Å

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