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BioAssay: AID 256641

Average Binding Constant for ABL2; NA=Not Active at 10 uM

Kinase inhibitors show great promise as a new class of therapeutics. Here we describe an efficient way to determine kinase inhibitor specificity by measuring binding of small molecules to the ATP site of kinases. We have profiled 20 kinase inhibitors, including 16 that are approved drugs or in clinical development, against a panel of 119 protein kinases. We find that specificity varies widely and more ..
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 Tested Compounds
 Tested Compounds
All(20)
 
 
Active(9)
 
 
Inactive(11)
 
 
 Tested Substances
 Tested Substances
All(21)
 
 
Active(10)
 
 
Inactive(11)
 
 
 Related BioAssays
 Related BioAssays
AID: 256641
Data Source: ChEMBL (325082)
BioAssay Type: Confirmatory, Concentration-Response Relationship Observed
Depositor Category: Literature, Extracted
BioAssay Version:
Deposit Date: 2010-05-24
Modify Date: 2014-08-24

Data Table ( Complete ):           View Active Data    View All Data
Target
Sequence: RecName: Full=Abelson tyrosine-protein kinase 2; AltName: Full=Abelson murine leukemia viral oncogene homolog 2; AltName: Full=Abelson-related gene protein; AltName: Full=Tyrosine-protein kinase ARG
Description ..   
Protein Family: Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase
Comment ..   

Gene:ABL2     Related Protein 3D Structures     More BioActivity Data..
BioActive Compounds: 9
Description:
Title: A small molecule-kinase interaction map for clinical kinase inhibitors.

Abstract: Kinase inhibitors show great promise as a new class of therapeutics. Here we describe an efficient way to determine kinase inhibitor specificity by measuring binding of small molecules to the ATP site of kinases. We have profiled 20 kinase inhibitors, including 16 that are approved drugs or in clinical development, against a panel of 119 protein kinases. We find that specificity varies widely and is not strongly correlated with chemical structure or the identity of the intended target. Many novel interactions were identified, including tight binding of the p38 inhibitor BIRB-796 to an imatinib-resistant variant of the ABL kinase, and binding of imatinib to the SRC-family kinase LCK. We also show that mutations in the epidermal growth factor receptor (EGFR) found in gefitinib-responsive patients do not affect the binding affinity of gefitinib or erlotinib. Our results represent a systematic small molecule-protein interaction map for clinical compounds across a large number of related proteins.
(PMID: 15711537)
Comment
Compounds with activity <= 50uM or explicitly reported as active by ChEMBL are flagged as active in this PubChem assay presentation.
Categorized Comment - additional comments and annotations
From BioAssay Depositor:
Assay Type: Binding
Target Type: Target is a single protein chain
Assay Data Source: Scientific Literature
Result Definitions
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TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1Kd*Kd PubChem standard valueFloatμM
3BEIBinding Efficiency Index(nM)Float
2SEISurface Efficiency Index(nM)Float
4LELigand EfficiencyFloat
5LLELipophilic Ligand EfficiencyFloat
6Kd activity commentKd activity commentString
7Kd standard flagKd standard flagInteger
8Kd qualifierKd qualifierString
9Kd published valueKd published valueFloatμM
10Kd standard valueKd standard valueFloatnM
11Kd binding domainsKd binding domainsString

* Activity Concentration.

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