Activity at human VDR expressed in human HOS cells transfected with pGL3-hOc, pCDNA-hVDR and phRL-TK assessed as assessed as transcriptional activation measured 24 hrs post infection by luciferase reporter gene assay - BioAssay Summary
We designed and synthesized nonsecosteroidal vitamin D receptor (VDR) ligands that formed H-bonds with six amino acid residues (Tyr143, Ser233, Arg270, Ser274, His301 and His393) of the VDR ligand-binding domain. The ligand YR335 exhibited potent transcriptional activity, which was comparable to those of 1##,25-dihydroxyvitamin D(3) and YR301. The crystal structure of the complex formed between YR335 and the VDR ligand-binding domain was solved, which revealed that YR335 formed H-bonds with the six amino acid residues mentioned above. ..more
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 Tested Compounds
 Tested Compounds
All(8)
 
 
Active(8)
 
 
 Tested Substances
 Tested Substances
All(8)
 
 
Active(8)
 
 
 Related BioAssays
 Related BioAssays
Table of Contents
AID: 622098
Data Source: ChEMBL (772109)
Depositor Category: Literature, Extracted
BioAssay Version:
Deposit Date: 2012-04-30
Modify Date: 2013-05-15

Data Table (Complete):           Active    All
Target
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Sequence: RecName: Full=Vitamin D3 receptor; Short=VDR; AltName: Full=1,25-dihydroxyvitamin D3 receptor; AltName: Full=Nuclear receptor subfamily 1 group I member 1
Description ..   
Protein Family: The ligand binding domain of vitamin D receptors, a member of the nuclear receptor superfamily
Comment ..   

Gene:VDR     Related Protein 3D Structures
BioActive Compounds: 8
Description:
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Title: Design, synthesis and X-ray crystallographic study of new nonsecosteroidal vitamin D receptor ligands.

Abstract: We designed and synthesized nonsecosteroidal vitamin D receptor (VDR) ligands that formed H-bonds with six amino acid residues (Tyr143, Ser233, Arg270, Ser274, His301 and His393) of the VDR ligand-binding domain. The ligand YR335 exhibited potent transcriptional activity, which was comparable to those of 1##,25-dihydroxyvitamin D(3) and YR301. The crystal structure of the complex formed between YR335 and the VDR ligand-binding domain was solved, which revealed that YR335 formed H-bonds with the six amino acid residues mentioned above.
(PMID: 21889334)
Comment
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Compounds with activity <= 50uM or explicitly reported as active by ChEMBL are flagged as active in this PubChem assay presentation.

Categorized Comment
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ChEMBL Assay Type: Binding

ChEMBL Assay Data Source: Scientific Literature

ChEMBL Target ID: 64

ChEMBL target type: Target is a single protein chain

Result Definitions
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TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1EC50*EC50 PubChem standard valueFloatμM
2BEIBinding Efficiency Index(nM)Float
3SEISurface Efficiency Index(nM)Float
4EC50 activity commentEC50 activity commentString
5EC50 standard flagEC50 standard flagInteger
6EC50 qualifierEC50 qualifierString
7EC50 published valueEC50 published valueFloatnM
8EC50 standard valueEC50 standard valueFloatnM
9EC50 data validityEC50 data validityString
10EC50 binding domainsEC50 binding domainsString
* Activity Concentration.

Data Table (Concise)
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Classification
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