2cdd: Difference between revisions

Revision as of 04:06, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2cdd.png

Template:STRUCTURE 2cdd

HUMAN HSP90 WITH 4-(4-(2,3-DIHYDRO-BENZOL(1,4)DIOXIN-6-YL)-5-METHYL-1H-PYRAZOL-3-YL)-6-ETHYL-BENZENE-1,3-DIOLHUMAN HSP90 WITH 4-(4-(2,3-DIHYDRO-BENZOL(1,4)DIOXIN-6-YL)-5-METHYL-1H-PYRAZOL-3-YL)-6-ETHYL-BENZENE-1,3-DIOL

Template:ABSTRACT PUBMED 16460658

About this StructureAbout this Structure

2CDD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

A fluorescence polarization assay for inhibitors of Hsp90., Howes R, Barril X, Dymock BW, Grant K, Northfield CJ, Robertson AG, Surgenor A, Wayne J, Wright L, James K, Matthews T, Cheung KM, McDonald E, Workman P, Drysdale MJ, Anal Biochem. 2006 Mar 15;350(2):202-13. Epub 2006 Jan 23. PMID:16460658

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2cdd|  PDB=2cdd  |  SCENE=  }}
-'''HUMAN HSP90 WITH 4-(4-(2,3-DIHYDRO-BENZOL(1,4)DIOXIN-6-YL)-5-METHYL-1H-PYRAZOL-3-YL)-6-ETHYL-BENZENE-1,3-DIOL'''
+===HUMAN HSP90 WITH 4-(4-(2,3-DIHYDRO-BENZOL(1,4)DIOXIN-6-YL)-5-METHYL-1H-PYRAZOL-3-YL)-6-ETHYL-BENZENE-1,3-DIOL===
-==Overview==
+<!--
-Hsp90 encodes a ubiquitous molecular chaperone protein conserved among species which acts on multiple substrates, many of which are important cell-signaling proteins. Inhibition of Hsp90 function has been promoted as a mechanism to degrade client proteins involved in tumorigenesis and disease progression. Several assays to monitor inhibition of Hsp90 function currently exist but are limited in their use for a drug discovery campaign. Using data from the crystal structure of an initial hit compound, we have developed a fluorescence polarization assay to monitor binding of compounds to the ATP-binding site of Hsp90. This assay is very robust (Z' &gt; 0.9) and can detect affinity of compounds with IC50s to 40 nM. We have used this assay in conjunction with cocrystal structures of small molecules to drive a structure-based design program aimed at the discovery and optimization of a novel class of potent Hsp90 inhibitors.
+The line below this paragraph, {{ABSTRACT_PUBMED_16460658}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16460658}}
 ==About this Structure==
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 [[Category: Phosphorylation]]
 [[Category: Pyrazole]]
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