View source for 1yet

[[Image:1yet.jpg|left|200px]]

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{{STRUCTURE_1yet|  PDB=1yet  |  SCENE=  }} 

'''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 [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YET 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:[http://www.ncbi.nlm.nih.gov/pubmed/9108479 9108479]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Pavletich, N P.]]
[[Category: Russo, A A.]]
[[Category: Stebbins, C E.]]
[[Category: Chaperone protein]]
[[Category: Geldanamycin]]
[[Category: Heat shock]]
[[Category: Signal transduction]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:14:03 2008''