1YES
HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "OPEN" CONFORMATION
Summary for 1YES
| Entry DOI | 10.2210/pdb1yes/pdb |
| Descriptor | HEAT SHOCK PROTEIN 90 (2 entities in total) |
| Functional Keywords | chaperone protein, geldanamycin, signal transduction, heat shock |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P07900 |
| Total number of polymer chains | 1 |
| Total formula weight | 25670.79 |
| Authors | Stebbins, C.E.,Russo, A.A.,Pavletich, N.P. (deposition date: 1997-03-25, release date: 1998-04-22, Last modification date: 2024-02-14) |
| Primary citation | Stebbins, C.E.,Russo, A.A.,Schneider, C.,Rosen, N.,Hartl, F.U.,Pavletich, N.P. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell(Cambridge,Mass.), 89:239-250, 1997 Cited by PubMed Abstract: 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. PubMed: 9108479DOI: 10.1016/S0092-8674(00)80203-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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