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ChEMBL ligand: CHEMBL501134 (Saxitoxin) |
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CHEMBL501134_lig_chart_3
Nav1.2
Rat
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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 |
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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]