1yet: Difference between revisions
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==GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN== | ==GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN== | ||
<StructureSection load='1yet' size='340' side='right' caption='[[1yet]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1yet' size='340' side='right' caption='[[1yet]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
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<table><tr><td colspan='2'>[[1yet]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. The December 2008 RCSB PDB [http://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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YET FirstGlance]. <br> | <table><tr><td colspan='2'>[[1yet]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. The December 2008 RCSB PDB [http://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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YET FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDM:GELDANAMYCIN'>GDM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDM:GELDANAMYCIN'>GDM</scene></td></tr> | ||
<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=1yet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yet OCA], [http://pdbe.org/1yet PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yet RCSB], [http://www.ebi.ac.uk/pdbsum/1yet PDBsum]</span></td></tr> | <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=1yet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yet OCA], [http://pdbe.org/1yet PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yet RCSB], [http://www.ebi.ac.uk/pdbsum/1yet PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yet ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ye/1yet_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ye/1yet_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 10:04, 25 April 2018
GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAINGELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN
Structural highlights
Function[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.[1] [2] 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 PubMedThe 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. 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:9108479[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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