1yes
From Proteopedia
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| - | [[Image:1yes.jpg|left|200px]] | + | [[Image:1yes.jpg|left|200px]] |
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| - | '''HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "OPEN" CONFORMATION''' | + | {{Structure |
| + | |PDB= 1yes |SIZE=350|CAPTION= <scene name='initialview01'>1yes</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "OPEN" CONFORMATION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YES is a [ | + | 1YES 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=1YES OCA]. |
==Reference== | ==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:// | + | 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: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:21:55 2008'' |
Revision as of 13:21, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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