1yet
From Proteopedia
Line 1: | Line 1: | ||
- | [[Image:1yet.jpg|left|200px]] | + | [[Image:1yet.jpg|left|200px]] |
- | + | ||
- | '''GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN''' | + | {{Structure |
+ | |PDB= 1yet |SIZE=350|CAPTION= <scene name='initialview01'>1yet</scene>, resolution 1.90Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=GDM:GELDANAMYCIN'>GDM</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN''' | ||
+ | |||
==Overview== | ==Overview== | ||
Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
- | 1YET is a [ | + | 1YET 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=1YET 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]] | ||
Line 22: | Line 31: | ||
[[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 15:21:56 2008'' |
Revision as of 13:21, 20 March 2008
| |||||||
, resolution 1.90Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | |||||||
Coordinates: | save as pdb, mmCIF, xml |
GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN
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
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
Page seeded by OCA on Thu Mar 20 15:21:56 2008