saxitoxin [Ligand Id: 2625] activity data from GtoPdb and ChEMBL

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ChEMBL ligand: CHEMBL501134 (Saxitoxin)
  • Nav1.4/Sodium channel protein type IV alpha subunit in Human [ChEMBL: CHEMBL2072] [GtoPdb: 581] [UniProtKB: P35499]
  • Nav1.4/Sodium channel protein type IV alpha subunit in Rat [ChEMBL: CHEMBL3509] [GtoPdb: 581] [UniProtKB: P15390]
  • This target only has 0 pki data point
1 CHEMBL501134_lig_chart_1 Sodium channel protein type IV alpha subunit HumanRat
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  • Nav1.7/Sodium channel protein type IX alpha subunit in Human [ChEMBL: CHEMBL4296] [GtoPdb: 584] [UniProtKB: Q15858]
  • This target only has 0 pki data point
2 CHEMBL501134_lig_chart_2 Sodium channel protein type IX alpha subunit Human
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  • Nav1.2 in Rat [GtoPdb: 579] [UniProtKB: P04775]
  • This target only has 0 pki data point
3 CHEMBL501134_lig_chart_3 Nav1.2 Rat
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  • Nav1.5 in Rat [GtoPdb: 582] [UniProtKB: P15389]
  • This target only has 0 pki data point
4 CHEMBL501134_lig_chart_4 Nav1.5 Rat
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DB Assay description Assay Type Standard value Standard parameter Original value Original units Original parameter Reference
Nav1.4/Sodium channel protein type IV alpha subunit in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL2072] [GtoPdb: 581] [UniProtKB: P35499]
ChEMBL Binding Assay: In initial studies, we designed a set of molecules with branching at the nitrogen of the carbamate side chain as well as the carbon adjacent to the nitrogen. Two mutant channels were also constructed by site-directed mutagenesis. The β-STXo1 data points were collected to demonstrate that STX and its derivatives were oriented similarly within the channel pore. The similar reductions in affinity for STX to β-STXo1 and for cyclohexyl STX to cyclohexyl β-STXo1 provide strong initial evidence that the two molecules both reside in a similar orientation in the channel pore. B 7.05 pIC50 90 nM IC50 US-9174999-B2. Methods and compositions for studying, imaging, and treating pain (2015)
ChEMBL Binding Assay: In initial studies, we designed a set of molecules with branching at the nitrogen of the carbamate side chain as well as the carbon adjacent to the nitrogen. Two mutant channels were also constructed by site-directed mutagenesis. The β-STXo1 data points were collected to demonstrate that STX and its derivatives were oriented similarly within the channel pore. The similar reductions in affinity for STX to β-STXo1 and for cyclohexyl STX to cyclohexyl β-STXo1 provide strong initial evidence that the two molecules both reside in a similar orientation in the channel pore. B 7.52 pIC50 30 nM IC50 US-9174999-B2. Methods and compositions for studying, imaging, and treating pain (2015)
Nav1.4/Sodium channel protein type IV alpha subunit in Rat (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3509] [GtoPdb: 581] [UniProtKB: P15390]
GtoPdb - - 8.4 pIC50 4.1 nM IC50 Biophys. J. (2001) 80: 698-706 [PMID:11159437]
ChEMBL Binding Assay: In initial studies, we designed a set of molecules with branching at the nitrogen of the carbamate side chain as well as the carbon adjacent to the nitrogen. Two mutant channels were also constructed by site-directed mutagenesis. The β-STXo1 data points were collected to demonstrate that STX and its derivatives were oriented similarly within the channel pore. The similar reductions in affinity for STX to β-STXo1 and for cyclohexyl STX to cyclohexyl β-STXo1 provide strong initial evidence that the two molecules both reside in a similar orientation in the channel pore. B 8.62 pIC50 2.4 nM IC50 US-9174999-B2. Methods and compositions for studying, imaging, and treating pain (2015)
Nav1.7/Sodium channel protein type IX alpha subunit in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4296] [GtoPdb: 584] [UniProtKB: Q15858]
ChEMBL Inhibition of human Nav1.7 expressed in CHO cells at holding potential of -100 mV by patch-clamp electrophysiology method B 6.15 pIC50 702 nM IC50 Bioorg Med Chem Lett (2018) 28: 3141-3149 [PMID:30139550]
GtoPdb - - 6.2 pIC50 702 nM IC50 Proc. Natl. Acad. Sci. U.S.A. (2012) 109: 18102-7 [PMID:23077250]
Nav1.2 in Rat [GtoPdb: 579] [UniProtKB: P04775]
GtoPdb - - 8.8 pIC50 1.7 nM IC50 Nature (2005) 434: 763-7 [PMID:15815630]
Nav1.5 in Rat [GtoPdb: 582] [UniProtKB: P15389]
GtoPdb - - 7.4 pKd - - - Am. J. Physiol. (1996) 270: C1522-31 [PMID:8967455];
FEBS Lett. (1990) 275: 195-200 [PMID:2175715]

ChEMBL data shown on this page come from version 27:

Gaulton A, Hersey A, Nowotka M, Bento AP, Chambers J, Mendez D, Mutowo P, Atkinson F, Bellis LJ, Cibrián-Uhalte E, Davies M, Dedman N, Karlsson A, Magariños MP, Overington JP, Papadatos G, Smit I, Leach AR. (2017) 'The ChEMBL database in 2017.' Nucleic Acids Res., 45(D1). DOI: 10.1093/nar/gkw1074. [PMCID:5210557]