1yet

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{{STRUCTURE_1yet| PDB=1yet | SCENE= }}
{{STRUCTURE_1yet| PDB=1yet | SCENE= }}
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'''GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN'''
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===GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9108479 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9108479}}
==About this Structure==
==About this Structure==
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[[Category: Heat shock]]
[[Category: Heat shock]]
[[Category: Signal transduction]]
[[Category: Signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:14:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:13:59 2008''

Revision as of 14:14, 28 July 2008

Image:1yet.png

Template:STRUCTURE 1yet

GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN

Template:ABSTRACT PUBMED 9108479

About this Structure

1YET is a Single protein structure of sequence from Homo sapiens. 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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