1elw

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(New page: 200px<br /> <applet load="1elw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1elw, resolution 1.60&Aring;" /> '''Crystal structure o...)
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[[Image:1elw.gif|left|200px]]<br />
 
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<applet load="1elw" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1elw, resolution 1.60&Aring;" />
 
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'''Crystal structure of the TPR1 domain of HOP in complex with a HSC70 peptide'''<br />
 
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==Overview==
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==Crystal structure of the TPR1 domain of HOP in complex with a HSC70 peptide==
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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.
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<StructureSection load='1elw' size='340' side='right'caption='[[1elw]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1elw]] is a 4 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=1ELW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELW FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#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=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1elw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elw OCA], [https://pdbe.org/1elw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elw RCSB], [https://www.ebi.ac.uk/pdbsum/1elw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/STIP1_HUMAN STIP1_HUMAN] Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/el/1elw_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1elw ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1ELW 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 TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ELW OCA].
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*[[HOP protein|HOP protein]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10786835 10786835]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Brinker, A.]]
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[[Category: Brinker A]]
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[[Category: Hartl, F.U.]]
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[[Category: Hartl FU]]
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[[Category: Moarefi, I.]]
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[[Category: Moarefi I]]
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[[Category: Scheufler, C.]]
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[[Category: Scheufler C]]
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[[Category: NI]]
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[[Category: TRS]]
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[[Category: helical repeat]]
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[[Category: hop]]
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[[Category: hsc70]]
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[[Category: hsp70]]
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[[Category: peptide-complex]]
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[[Category: protein binding]]
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[[Category: tpr-domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:44:44 2007''
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Current revision

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

PDB ID 1elw

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