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1yer

From Proteopedia

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{{STRUCTURE_1yer| PDB=1yer | SCENE= }}
{{STRUCTURE_1yer| PDB=1yer | SCENE= }}
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'''HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "CLOSED" CONFORMATION'''
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===HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "CLOSED" CONFORMATION===
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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]]
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Revision as of 10:03, 29 July 2008

Image:1yer.png

Template:STRUCTURE 1yer

HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "CLOSED" CONFORMATION

Template:ABSTRACT PUBMED 9108479

About this Structure

1YER 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

Page seeded by OCA on Tue Jul 29 13:02:56 2008

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