Target Information

General Information of This Target
Target ID
BTDT10233
Target Name
Potassium voltage-gated channel
Target Bioclass
Transporter and channel
Taxonomy ID
10116
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Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Rodentia
Family: Muridae
Genus: Rattus
Species: Rattus norvegicus
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Kappa-conotoxin Mo1659 . . [1]
 Toxin Info    Cysteine-rich venom protein helothermine . . [2], [3], [4], [5]
 Toxin Info    MgTX Dissociation constant
0.07 pM
 [6]
 Toxin Info    HgTX1 (A19Y,Y37F) Dissociation constant
0.15 pM
 [7]
 Toxin Info    Venom basic protease inhibitor 1 homolog (L3R,Q18D,G34R,T36D,R59G) Dissociation constant
5 pM
 [8]
 Toxin Info    Peptide 401 Dissociation constant
0.115 nM
 [9]
 Toxin Info    BmTX3A Dissociation constant
0.21 nM
 [10]
 Toxin Info    ChTX Dissociation constant
0.29 nM
 [11]
 Toxin Info    Venom basic protease inhibitor 1 homolog (L3R,Q18D,G34R,T36D,R59G) Dissociation constant
0.3 nM
 [12]
 Toxin Info    Venom basic protease inhibitor 1 homolog (L3R,Q18D,G34R,T36D,R59G) Dissociation constant
0.5 nM
 [13]
 Toxin Info    Beta-1-bungarotoxin Dissociation constant
0.6 nM
 [14]
 Toxin Info    Beta-1-bungarotoxin Dissociation constant
0.7 nM
 [13]
 Toxin Info    Venom basic protease inhibitor 1 homolog Dissociation constant
0.96 nM
 [9]
 Toxin Info    Delta/kappa-actitoxin-Avd4a Dissociation constant
12 nM
 [15- 20]
 Toxin Info    DeltaKappa-actitoxin-Avd4b Dissociation constant
19 nM
 [15], [16], [18]
 Toxin Info    Conotoxin Vr3a Inhibition rate
10 %
 [21]
 Toxin Info    Mu-theraphotoxin-Cg1a Inhibition rate
22 %
 [22], [23], [24], [25]
 Toxin Info    Beta/kappa-theraphotoxin-Cg2a IC50
52.3 nM
 [22- 29]
 Toxin Info    Pi-phymatoxin-Pcf1a IC50
3.5 μM
 [30]
 Toxin Info    Toxin PhcrTx2 IC50
6.4 μM
 [31]
References
Ref 1 A novel 13 residue acyclic peptide from the marine snail, Conus monile, targets potassium channels. Biochem Biophys Res Commun. 2004 May 7;317(3):682-8. doi: 10.1016/j.bbrc.2004.03.100.
Ref 2 Primary structure and properties of helothermine, a peptide toxin that blocks ryanodine receptors. Biophys J. 1995 Jun;68(6):2280-8. doi: 10.1016/S0006-3495(95)80410-8.
Ref 3 Isolation and characterization of helothermine, a novel toxin from Heloderma horridum horridum (Mexican beaded lizard) venom. Toxicon. 1990;28(3):299-309. doi: 10.1016/0041-0101(90)90065-f.
Ref 4 The toxin helothermine affects potassium currents in newborn rat cerebellar granule cells. J Membr Biol. 1994 Apr;139(1):49-55. doi: 10.1007/BF00232674.
Ref 5 Helothermine, a lizard venom toxin, inhibits calcium current in cerebellar granules. Exp Brain Res. 1996 Jun;110(1):15-20. doi: 10.1007/BF00241369.
Ref 6 [125I]margatoxin, an extraordinarily high affinity ligand for voltage-gated potassium channels in mammalian brain. Biochemistry. 1995 Oct 17;34(41):13627-34. doi: 10.1021/bi00041a043.
Ref 7 Subunit composition of brain voltage-gated potassium channels determined by hongotoxin-1, a novel peptide derived from Centruroides limbatus venom. J Biol Chem. 1998 Jan 30;273(5):2639-44. doi: 10.1074/jbc.273.5.2639.
Ref 8 Delineation of the functional site of alpha-dendrotoxin. The functional topographies of dendrotoxins are different but share a conserved core with those of other Kv1 potassium channel-blocking toxins. J Biol Chem. 1998 Sep 25;273(39):25393-403. doi: 10.1074/jbc.273.39.25393.
Ref 9 The receptor site for the bee venom mast cell degranulating peptide. Affinity labeling and evidence for a common molecular target for mast cell degranulating peptide and dendrotoxin I, a snake toxin active on K+ channels. Biochemistry. 1988 Mar 22;27(6):1827-32. doi: 10.1021/bi00406a005.
Ref 10 Definition of the alpha-KTx15 subfamily. Toxicon. 2004 Jun 15;43(8):887-94. doi: 10.1016/j.toxicon.2004.03.023.
Ref 11 Characterization of high affinity binding sites for charybdotoxin in synaptic plasma membranes from rat brain. Evidence for a direct association with an inactivating, voltage-dependent, potassium channel. J Biol Chem. 1990 Sep 15;265(26):15564-71.
Ref 12 Involvement of neuronal acceptors for dendrotoxin in its convulsive action in rat brain. Biochem J. 1986 Jul 15;237(2):397-404. doi: 10.1042/bj2370397.
Ref 13 Solubilization and physical characterization of acceptors for dendrotoxin and beta-bungarotoxin from synaptic membranes of rat brain. Biochemistry. 1988 Sep 6;27(18):6814-20. doi: 10.1021/bi00418a025.
Ref 14 Preparation of neurotoxic 3H-beta-bungarotoxin: demonstration of saturable binding to brain synapses and its inhibition by toxin I. Eur J Biochem. 1982 Nov;128(1):267-76. doi: 10.1111/j.1432-1033.1982.tb06961.x.
Ref 15 Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4. J Biol Chem. 1998 Mar 20;273(12):6744-9. doi: 10.1074/jbc.273.12.6744.
Ref 16 Modulation of Kv3 subfamily potassium currents by the sea anemone toxin BDS: significance for CNS and biophysical studies. J Neurosci. 2005 Sep 21;25(38):8735-45. doi: 10.1523/JNEUROSCI.2119-05.2005.
Ref 17 Modulation of neuronal sodium channels by the sea anemone peptide BDS-I. J Neurophysiol. 2012 Jun;107(11):3155-67. doi: 10.1152/jn.00785.2011. Epub 2012 Mar 21.
Ref 18 Development of a rational nomenclature for naming peptide and protein toxins from sea anemones. Toxicon. 2012 Sep 15;60(4):539-50. doi: 10.1016/j.toxicon.2012.05.020. Epub 2012 Jun 5.
Ref 19 A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structure. Biochemistry. 1989 Mar 7;28(5):2178-87. doi: 10.1021/bi00431a032.
Ref 20 Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry. 1989 Mar 7;28(5):2188-98. doi: 10.1021/bi00431a033.
Ref 21 A novel proline-rich M-superfamily conotoxin that can simultaneously affect sodium, potassium and calcium currents. J Venom Anim Toxins Incl Trop Dis. 2021 Jun 11;27:e20200164. doi: 10.1590/1678-9199-JVATITD-2020-0164. eCollection 2021.
Ref 22 Molecular diversity and evolution of cystine knot toxins of the tarantula Chilobrachys jingzhao. Cell Mol Life Sci. 2008 Aug;65(15):2431-44. doi: 10.1007/s00018-008-8135-x.
Ref 23 Proteomic and peptidomic analysis of the venom from Chinese tarantula Chilobrachys jingzhao. Proteomics. 2007 Jun;7(11):1892-907. doi: 10.1002/pmic.200600785.
Ref 24 Expression and characterization of jingzhaotoxin-34, a novel neurotoxin from the venom of the tarantula Chilobrachys jingzhao. Peptides. 2009 Jun;30(6):1042-8. doi: 10.1016/j.peptides.2009.02.018. Epub 2009 Mar 13.
Ref 25 Selective Closed-State Nav1.7 Blocker JZTX-34 Exhibits Analgesic Effects against Pain. Toxins (Basel). 2018 Feb 2;10(2):64. doi: 10.3390/toxins10020064.
Ref 26 Isolation and characterization of Jingzhaotoxin-V, a novel neurotoxin from the venom of the spider Chilobrachys jingzhao. Toxicon. 2007 Mar 1;49(3):388-99. doi: 10.1016/j.toxicon.2006.10.012. Epub 2006 Nov 6.
Ref 27 Effects and mechanism of Chinese tarantula toxins on the Kv2.1 potassium channels. Biochem Biophys Res Commun. 2007 Jan 19;352(3):799-804. doi: 10.1016/j.bbrc.2006.11.086. Epub 2006 Nov 27.
Ref 28 Molecular surface of JZTX-V (-Theraphotoxin-Cj2a) interacting with voltage-gated sodium channel subtype NaV1.4. Toxins (Basel). 2014 Jul 23;6(7):2177-93. doi: 10.3390/toxins6072177.
Ref 29 Pharmacological characterization of potent and selective NaV1.7 inhibitors engineered from Chilobrachys jingzhao tarantula venom peptide JzTx-V. PLoS One. 2018 May 3;13(5):e0196791. doi: 10.1371/journal.pone.0196791. eCollection 2018.
Ref 30 A novel sea anemone peptide that inhibits acid-sensing ion channels. Peptides. 2014 Mar;53:3-12. doi: 10.1016/j.peptides.2013.06.003. Epub 2013 Jun 10.
Ref 31 PhcrTx2, a New Crab-Paralyzing Peptide Toxin from the Sea Anemone Phymanthus crucifer. Toxins (Basel). 2018 Feb 7;10(2):72. doi: 10.3390/toxins10020072.
Ref 32 The characterization of high-affinity binding sites in rat brain for the mast cell-degranulating peptide from bee venom using the purified monoiodinated peptide. J Biol Chem. 1984 Nov 25;259(22):13957-67.
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