TargetCalmodulin-domain protein kinase 1(Toxoplasma gondii)
University of Washington Through Its Center For Commercialization
US Patent
University of Washington Through Its Center For Commercialization
US Patent
Affinity DataIC50: 8nMAssay Description:Inhibition of TgCDPK1 and CpCDPK1 was determined using a luminescent kinase assay which measures ATP depletion in the presence of the Syntide 2 pepti...More data for this Ligand-Target Pair
3D Structure (crystal)TargetCalmodulin-domain protein kinase 1(Toxoplasma gondii)
University of Washington Through Its Center For Commercialization
US Patent
University of Washington Through Its Center For Commercialization
US Patent
Affinity DataIC50: 8nMAssay Description:Inhibition of TgCDPK1 and CpCDPK1 was determined using a luminescent kinase assay which measures ATP depletion in the presence of the Syntide 2 pepti...More data for this Ligand-Target Pair
TargetCalmodulin-domain protein kinase 1(Toxoplasma gondii)
University of Washington Through Its Center For Commercialization
US Patent
University of Washington Through Its Center For Commercialization
US Patent
Affinity DataIC50: 15nMAssay Description:Inhibition of TgCDPK1 and CpCDPK1 was determined using a luminescent kinase assay which measures ATP depletion in the presence of the Syntide 2 pepti...More data for this Ligand-Target Pair
TargetCalmodulin-domain protein kinase 1(Toxoplasma gondii)
University of Washington Through Its Center For Commercialization
US Patent
University of Washington Through Its Center For Commercialization
US Patent
Affinity DataIC50: 15nMAssay Description:Inhibition of Toxoplasma gondii recombinant N-terminal hexahistidine tagged CDPK1 expressed in Escherichia coli using syntide-2 as substrate after 90...More data for this Ligand-Target Pair
TargetCalmodulin-domain protein kinase 1(Toxoplasma gondii)
University of Washington Through Its Center For Commercialization
US Patent
University of Washington Through Its Center For Commercialization
US Patent
Affinity DataIC50: 15nMAssay Description:Most known kinase inhibitors bind in the ATP-binding pocket of the active site19,20. These inhibitors exploit many of the same hydrophobic contacts a...More data for this Ligand-Target Pair
