1yet | pdb_00001yet

GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN

spinqualitylabelsall models 1yet, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1yet is a 1 chain structure with sequence from Homo sapiens. The December 2008 RCSB PDB Molecule of the Month feature on Hsp90 by David Goodsell is 10.2210/rcsb_pdb/mom_2008_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GDM Resources: FirstGlance, OCA, RCSB, PDBsum 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 PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Heat Shock Proteins

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