1yet
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(New page: 200px<br /> <applet load="1yet" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yet, resolution 1.90Å" /> '''GELDANAMYCIN BOUND ...)
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Revision as of 18:12, 12 November 2007
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GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN
Overview
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 Structure
1YET is a Single protein structure of sequence from Homo sapiens with GDM as ligand. Full crystallographic information is available from OCA.
Reference
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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