1yet: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1yet PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yet RCSB]</span>
}}
}}


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[[Category: Russo, A A.]]
[[Category: Russo, A A.]]
[[Category: Stebbins, C E.]]
[[Category: Stebbins, C E.]]
[[Category: GDM]]
[[Category: chaperone protein]]
[[Category: chaperone protein]]
[[Category: geldanamycin]]
[[Category: geldanamycin]]
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[[Category: signal transduction]]
[[Category: signal transduction]]


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Revision as of 01:05, 31 March 2008

File:1yet.jpg


PDB ID 1yet

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN


OverviewOverview

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.

About this StructureAbout this Structure

1YET is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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

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