1yes
From Proteopedia
(New page: 200px<br /> <applet load="1yes" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yes, resolution 2.20Å" /> '''HUMAN HSP90 GELDANA...) |
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- | [[Image:1yes. | + | [[Image:1yes.jpg|left|200px]]<br /><applet load="1yes" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1yes, resolution 2.20Å" /> | caption="1yes, resolution 2.20Å" /> | ||
'''HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "OPEN" CONFORMATION'''<br /> | '''HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "OPEN" CONFORMATION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
- | 1YES is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1YES is a [http://en.wikipedia.org/wiki/Single_protein 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=1YES OCA]. |
==Reference== | ==Reference== | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:11:59 2008'' |
Revision as of 15:11, 15 February 2008
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HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "OPEN" CONFORMATION
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
1YES 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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