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BioAssay: AID 649220

Agonist activity at N-terminal His-tagged human PPARgamma expressed in Escherichia coli BL21 assessed as transactivation activity

Human peroxisome proliferator-activated receptors (hPPARs) are ligand-dependent transcription factors that control various biological responses, and there are three subtypes: hPPARalpha, hPPARdelta, and hPPARgamma. We report here that alpha-substituted phenylpropanoic acid-type hPPAR agonists with similar structure bind to the hPPAR ligand binding domain (LBD) in different conformations, depending on the receptor subtype. These results might indicate that hPPAR ligand binding pockets have multiple binding points that can be utilized to accommodate structurally flexible hPPAR ligands. ..more
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 Tested Compounds
 Tested Compounds
All(1)
 
 
Inactive(1)
 
 
 Tested Substances
 Tested Substances
All(1)
 
 
Inactive(1)
 
 
 Related BioAssays
 Related BioAssays
AID: 649220
Data Source: ChEMBL (806668)
Depositor Category: Literature, Extracted
BioAssay Version:
Deposit Date: 2012-09-09
Modify Date: 2014-05-26

Data Table ( Complete ):           View All Data
Target
Sequence: RecName: Full=Peroxisome proliferator-activated receptor gamma; Short=PPAR-gamma; AltName: Full=Nuclear receptor subfamily 1 group C member 3
Description ..   
Protein Family: The ligand binding domain of peroxisome proliferator-activated receptors
Comment ..   

Gene:PPARG     Related Protein 3D Structures     More BioActivity Data..
Tested Compound:
Description:
Title: Peroxisome proliferator-activated receptors (PPARs) have multiple binding points that accommodate ligands in various conformations: phenylpropanoic acid-type PPAR ligands bind to PPAR in different conformations, depending on the subtype.

Abstract: Human peroxisome proliferator-activated receptors (hPPARs) are ligand-dependent transcription factors that control various biological responses, and there are three subtypes: hPPARalpha, hPPARdelta, and hPPARgamma. We report here that alpha-substituted phenylpropanoic acid-type hPPAR agonists with similar structure bind to the hPPAR ligand binding domain (LBD) in different conformations, depending on the receptor subtype. These results might indicate that hPPAR ligand binding pockets have multiple binding points that can be utilized to accommodate structurally flexible hPPAR ligands.
(PMID: 22185225)
Categorized Comment
Assay Type: Functional

Assay Data Source: Scientific Literature

Target Type: Target is a single protein chain

Result Definitions
TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1EC50 activity commentEC50 activity commentString
2EC50 standard flagEC50 standard flagInteger
3EC50 qualifierEC50 qualifierString
4EC50 published valueEC50 published valueFloat
5EC50 standard valueEC50 standard valueFloat

Data Table (Concise)
Data Table ( Complete ):     View All Data
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