1yes: Difference between revisions

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[[Image:1yes.jpg|left|200px]]
{{Seed}}
[[Image:1yes.png|left|200px]]


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{{STRUCTURE_1yes|  PDB=1yes  |  SCENE=  }}  
{{STRUCTURE_1yes|  PDB=1yes  |  SCENE=  }}  


'''HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "OPEN" CONFORMATION'''
===HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "OPEN" CONFORMATION===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_9108479}}, adds the Publication Abstract to the page
(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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