1elr: Difference between revisions

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<StructureSection load='1elr' size='340' side='right'caption='[[1elr]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1elr' size='340' side='right'caption='[[1elr]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1elr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
<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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
</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>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
<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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1elw|1elw]]</div></td></tr>
<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>
<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>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/STIP1_HUMAN STIP1_HUMAN]] Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB).  
[https://www.uniprot.org/uniprot/STIP1_HUMAN STIP1_HUMAN] Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:10786835</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1elr" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[HOP protein|HOP protein]]
*[[HOP protein|HOP protein]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[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: Chaperone]]
[[Category: Helical repeat]]
[[Category: Hop]]
[[Category: Hsp90]]
[[Category: Peptide-complex]]
[[Category: Protein binding]]
[[Category: Tpr-domain]]

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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