1yet

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[[Image:1yet.jpg|left|200px]]<br /><applet load="1yet" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yet.jpg|left|200px]]
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caption="1yet, resolution 1.90&Aring;" />
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'''GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN'''<br />
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{{Structure
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|PDB= 1yet |SIZE=350|CAPTION= <scene name='initialview01'>1yet</scene>, resolution 1.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=GDM:GELDANAMYCIN'>GDM</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN-BINDING DOMAIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1YET is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GDM:'>GDM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YET OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9108479 9108479]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:44 2008''
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''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


PDB ID 1yet

Drag the structure with the mouse to rotate
, 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

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