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1yet

From Proteopedia

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[[Image:1yet.jpg|left|200px]]
 
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==GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN==
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The line below this paragraph, containing "STRUCTURE_1yet", creates the "Structure Box" on the page.
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<StructureSection load='1yet' size='340' side='right'caption='[[1yet]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1yet]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The December 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Hsp90'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_12 10.2210/rcsb_pdb/mom_2008_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YET 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]] 1.9&#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=GDM:GELDANAMYCIN'>GDM</scene></td></tr>
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{{STRUCTURE_1yet| PDB=1yet | SCENE= }}
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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=1yet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yet OCA], [https://pdbe.org/1yet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yet RCSB], [https://www.ebi.ac.uk/pdbsum/1yet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yet ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>
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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/ye/1yet_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=1yet ConSurf].
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<div style="clear:both"></div>
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'''GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN'''
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
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== References ==
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==Overview==
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<references/>
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The Hsp90 chaperone is required for the activation of several families of eukaryotic protein kinases and nuclear hormone receptors, many of which are protooncogenic and play a prominent role in cancer. The geldanamycin antibiotic has antiproliferative and antitumor effects, as it binds to Hsp90, inhibits the Hsp90-mediated conformational maturation/refolding reaction, and results in the degradation of Hsp90 substrates. The structure of the geldanamycin-binding domain of Hsp90 (residues 9-232) reveals a pronounced pocket, 15 A deep, that is highly conserved across species. Geldanamycin binds inside this pocket, adopting a compact structure similar to that of a polypeptide chain in a turn conformation. This, and the pocket's similarity to substrate-binding sites, suggest that the pocket binds a portion of the polypeptide substrate and participates in the conformational maturation/refolding reaction.
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__TOC__
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</StructureSection>
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==About this Structure==
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1YET 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=1YET OCA].
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==Reference==
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Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent., Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP, Cell. 1997 Apr 18;89(2):239-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9108479 9108479]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Hsp90]]
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[[Category: Pavletich, N P.]]
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[[Category: Large Structures]]
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[[Category: Russo, A A.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Stebbins, C E.]]
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[[Category: Pavletich NP]]
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[[Category: Chaperone protein]]
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[[Category: Russo AA]]
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[[Category: Geldanamycin]]
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[[Category: Stebbins CE]]
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[[Category: Heat shock]]
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[[Category: Signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:14:03 2008''
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Current revision

GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN

PDB ID 1yet

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