General Information of This Target
Target ID
BTDT10191
Target Name
Potassium voltage-gated channel subfamily A member 5
Target Bioclass
Transporter and channel
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N.A.
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    HgTX1 (A19Y,Y37F) . . [1]
 Toxin Info    Potassium channel toxin alpha-KTx 1.1 Dissociation constant
>100 nM
[2- 22]
 Toxin Info    U-scoloptoxin(15)-Sm2a Effect . [23], [24]
 Toxin Info    Venom peptide Sh41 Effect . [25]
 Toxin Info    Venom peptide Sh42 Effect . [25]
 Toxin Info    Neurotoxic enhancer CSTX-13 Inhibition rate . [26], [27], [28], [29]
 Toxin Info    Conopeptide Y-Pl1 Inhibition rate . [30]
 Toxin Info    Kappa-theraphotoxin-Ps1a Inhibition rate . [31], [32], [33]
 Toxin Info    Kappa-theraphotoxin-Ps1b Inhibition rate . [31]
 Toxin Info    Conopeptide Y-Fe1 Inhibition rate . [30]
 Toxin Info    Delta/kappa-actitoxin-Avd4a Inhibition rate . [34- 39]
 Toxin Info    Mambaquaretin-1 Inhibition rate . [40], [41], [42]
 Toxin Info    Potassium channel toxin alpha-KTx 1.16 Inhibition rate . [43], [44]
 Toxin Info    Potassium channel toxin alpha-KTx 1.17 Inhibition rate . [43], [44]
 Toxin Info    Kappa-actitoxin-Ael2a Inhibition rate . [37- 50]
 Toxin Info    Potassium channel toxin kappa-KTx 1.2 Inhibition rate . [51- 55]
 Toxin Info    Alpha/kappa-conotoxin pl14a Inhibition rate . [56]
 Toxin Info    Conopeptide Y-Pl1 IC50
>5 μM
[30]
 Toxin Info    Conopeptide Y-Fe1 IC50
>50 μM
[30]
References
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Ref 2 Dynamic diversification from a putative common ancestor of scorpion toxins affecting sodium, potassium, and chloride channels. J Mol Evol. 1999 Feb;48(2):187-96. doi: 10.1007/pl00006457.
Ref 3 Purification, sequence, and model structure of charybdotoxin, a potent selective inhibitor of calcium-activated potassium channels. Proc Natl Acad Sci U S A. 1988 May;85(10):3329-33. doi: 10.1073/pnas.85.10.3329.
Ref 4 Charybdotoxin is a new member of the K+ channel toxin family that includes dendrotoxin I and mast cell degranulating peptide. Biochemistry. 1989 Dec 12;28(25):9708-14. doi: 10.1021/bi00451a025.
Ref 5 Analysis of the blocking activity of charybdotoxin homologs and iodinated derivatives against Ca2+-activated K+ channels. J Membr Biol. 1989 Aug;109(3):269-81. doi: 10.1007/BF01870284.
Ref 6 Solution synthesis of charybdotoxin (ChTX), a K+ channel blocker. Biochem Biophys Res Commun. 1990 Jul 31;170(2):684-90. doi: 10.1016/0006-291x(90)92145-p.
Ref 7 Synthesis and structural characterization of charybdotoxin, a potent peptidyl inhibitor of the high conductance Ca2(+)-activated K+ channel. J Biol Chem. 1990 Nov 5;265(31):18745-8.
Ref 8 Purification and characterization of three inhibitors of voltage-dependent K+ channels from Leiurus quinquestriatus var. hebraeus venom. Biochemistry. 1994 Jun 7;33(22):6834-9. doi: 10.1021/bi00188a012.
Ref 9 Pharmacological characterization of five cloned voltage-gated K+ channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. Mol Pharmacol. 1994 Jun;45(6):1227-34.
Ref 10 BeKm-1 is a HERG-specific toxin that shares the structure with ChTx but the mechanism of action with ErgTx1. Biophys J. 2003 May;84(5):3022-36. doi: 10.1016/S0006-3495(03)70028-9.
Ref 11 Maurotoxin: a potent inhibitor of intermediate conductance Ca2+-activated potassium channels. Mol Pharmacol. 2003 Feb;63(2):409-18. doi: 10.1124/mol.63.2.409.
Ref 12 Multidimensional signatures in antimicrobial peptides. Proc Natl Acad Sci U S A. 2004 May 11;101(19):7363-8. doi: 10.1073/pnas.0401567101. Epub 2004 Apr 26.
Ref 13 A designer ligand specific for Kv1.3 channels from a scorpion neurotoxin-based library. Proc Natl Acad Sci U S A. 2009 Dec 29;106(52):22211-6. doi: 10.1073/pnas.0910123106. Epub 2009 Dec 10.
Ref 14 Scorpion Potassium Channel-blocking Defensin Highlights a Functional Link with Neurotoxin. J Biol Chem. 2016 Mar 25;291(13):7097-106. doi: 10.1074/jbc.M115.680611. Epub 2016 Jan 27.
Ref 15 Scorpion toxins interact with nicotinic acetylcholine receptors. FEBS Lett. 2019 Oct;593(19):2779-2789. doi: 10.1002/1873-3468.13530. Epub 2019 Jul 18.
Ref 16 Molecular structure of charybdotoxin, a pore-directed inhibitor of potassium ion channels. Science. 1990 Aug 3;249(4968):521-4. doi: 10.1126/science.1696395.
Ref 17 Molecular structure of charybdotoxin: retraction. Science. 1991 May 3;252(5006):631. doi: 10.1126/science.252.5006.631.b.
Ref 18 Three-dimensional structure of natural charybdotoxin in aqueous solution by 1H-NMR. Charybdotoxin possesses a structural motif found in other scorpion toxins. Eur J Biochem. 1991 Feb 26;196(1):19-28. doi: 10.1111/j.1432-1033.1991.tb15780.x.
Ref 19 Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins. Science. 1991 Dec 6;254(5037):1521-3. doi: 10.1126/science.1720574.
Ref 20 Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications. Biochemistry. 1992 Sep 1;31(34):7756-64. doi: 10.1021/bi00149a003.
Ref 21 Progress in multidimensional NMR investigations of peptide and protein 3-D structures in solution. From structure to functional aspects. Biochimie. 1992 Sep-Oct;74(9-10):825-36. doi: 10.1016/0300-9084(92)90065-m.
Ref 22 NMR solution structure of a two-disulfide derivative of charybdotoxin: structural evidence for conservation of scorpion toxin alpha/beta motif and its hydrophobic side chain packing. Biochemistry. 1997 Apr 1;36(13):3760-6. doi: 10.1021/bi962720h.
Ref 23 Clawing through evolution: toxin diversification and convergence in the ancient lineage Chilopoda (centipedes). Mol Biol Evol. 2014 Aug;31(8):2124-48. doi: 10.1093/molbev/msu162. Epub 2014 May 20.
Ref 24 A Centipede Toxin Family Defines an Ancient Class of CS Defensins. Structure. 2019 Feb 5;27(2):315-326.e7. doi: 10.1016/j.str.2018.10.022. Epub 2018 Dec 13.
Ref 25 Isolation and characterization of FMRFamide-like peptides in the venoms of solitary sphecid wasps. Peptides. 2021 Aug;142:170575. doi: 10.1016/j.peptides.2021.170575. Epub 2021 May 20.
Ref 26 The Dual Prey-Inactivation Strategy of Spiders-In-Depth Venomic Analysis of Cupiennius salei. Toxins (Basel). 2019 Mar 19;11(3):167. doi: 10.3390/toxins11030167.
Ref 27 CSTX-13, a highly synergistically acting two-chain neurotoxic enhancer in the venom of the spider Cupiennius salei (Ctenidae). Proc Natl Acad Sci U S A. 2004 Aug 3;101(31):11251-6. doi: 10.1073/pnas.0402226101. Epub 2004 Jul 22.
Ref 28 Spider venom: enhancement of venom efficacy mediated by different synergistic strategies in Cupiennius salei. J Exp Biol. 2005 Jun;208(Pt 11):2115-21. doi: 10.1242/jeb.01594.
Ref 29 Neurotoxin Merging: A Strategy Deployed by the Venom of the Spider Cupiennius salei to Potentiate Toxicity on Insects. Toxins (Basel). 2020 Apr 12;12(4):250. doi: 10.3390/toxins12040250.
Ref 30 Tyrosine-rich conopeptides affect voltage-gated K+ channels. J Biol Chem. 2008 Aug 22;283(34):23026-32. doi: 10.1074/jbc.M800084200. Epub 2008 May 27.
Ref 31 Effects of phrixotoxins on the Kv4 family of potassium channels and implications for the role of Ito1 in cardiac electrogenesis. Br J Pharmacol. 1999 Jan;126(1):251-63. doi: 10.1038/sj.bjp.0702283.
Ref 32 Studies examining the relationship between the chemical structure of protoxin II and its activity on voltage gated sodium channels. J Med Chem. 2014 Aug 14;57(15):6623-31. doi: 10.1021/jm500687u. Epub 2014 Jul 24.
Ref 33 Solution structure of Phrixotoxin 1, a specific peptide inhibitor of Kv4 potassium channels from the venom of the theraphosid spider Phrixotrichus auratus. Protein Sci. 2004 May;13(5):1197-208. doi: 10.1110/ps.03584304.
Ref 34 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 35 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 36 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 37 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 38 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 39 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 40 Green mamba peptide targets type-2 vasopressin receptor against polycystic kidney disease. Proc Natl Acad Sci U S A. 2017 Jul 3;114(27):7154-7159. doi: 10.1073/pnas.1620454114. Epub 2017 Jun 19.
Ref 41 A snake toxin as a theranostic agent for the type 2 vasopressin receptor. Theranostics. 2020 Sep 18;10(25):11580-11594. doi: 10.7150/thno.47485. eCollection 2020.
Ref 42 A new Kunitz-type snake toxin family associated with an original mode of interaction with the vasopressin 2 receptor. Br J Pharmacol. 2022 Jul;179(13):3470-3481. doi: 10.1111/bph.15814. Epub 2022 Feb 28.
Ref 43 Variability of Potassium Channel Blockers in Mesobuthus eupeus Scorpion Venom with Focus on Kv1.1: AN INTEGRATED TRANSCRIPTOMIC AND PROTEOMIC STUDY. J Biol Chem. 2015 May 8;290(19):12195-209. doi: 10.1074/jbc.M115.637611. Epub 2015 Mar 19.
Ref 44 K(V)1.2 channel-specific blocker from Mesobuthus eupeus scorpion venom: Structural basis of selectivity. Neuropharmacology. 2018 Dec;143:228-238. doi: 10.1016/j.neuropharm.2018.09.030. Epub 2018 Sep 22.
Ref 45 APETx1, a new toxin from the sea anemone Anthopleura elegantissima, blocks voltage-gated human ether-a-go-go-related gene potassium channels. Mol Pharmacol. 2003 Jul;64(1):59-69. doi: 10.1124/mol.64.1.59.
Ref 46 Species diversity and peptide toxins blocking selectivity of ether-a-go-go-related gene subfamily K+ channels in the central nervous system. Mol Pharmacol. 2006 May;69(5):1673-83. doi: 10.1124/mol.105.019729. Epub 2006 Feb 23.
Ref 47 APETx1 from sea anemone Anthopleura elegantissima is a gating modifier peptide toxin of the human ether-a-go-go- related potassium channel. Mol Pharmacol. 2007 Aug;72(2):259-68. doi: 10.1124/mol.107.035840. Epub 2007 May 1.
Ref 48 A natural point mutation changes both target selectivity and mechanism of action of sea anemone toxins. FASEB J. 2012 Dec;26(12):5141-51. doi: 10.1096/fj.12-218479. Epub 2012 Sep 12.
Ref 49 Defensin-neurotoxin dyad in a basally branching metazoan sea anemone. FEBS J. 2017 Oct;284(19):3320-3338. doi: 10.1111/febs.14194. Epub 2017 Sep 6.
Ref 50 Solution structure of APETx1 from the sea anemone Anthopleura elegantissima: a new fold for an HERG toxin. Proteins. 2005 May 1;59(2):380-6. doi: 10.1002/prot.20425.
Ref 51 kappa-Hefutoxin1, a novel toxin from the scorpion Heterometrus fulvipes with unique structure and function. Importance of the functional diad in potassium channel selectivity. J Biol Chem. 2002 Aug 16;277(33):30040-7. doi: 10.1074/jbc.M111258200. Epub 2002 May 28.
Ref 52 Synthesis and characterization of amino acid deletion analogs of -hefutoxin 1, a scorpion toxin on potassium channels. Toxicon. 2013 Sep;71:25-30. doi: 10.1016/j.toxicon.2013.05.010. Epub 2013 May 29.
Ref 53 Expanding the pharmacological profile of -hefutoxin 1 and analogues: A focus on the inhibitory effect on the oncogenic channel K(v)10.1. Peptides. 2017 Dec;98:43-50. doi: 10.1016/j.peptides.2016.08.008. Epub 2016 Aug 28.
Ref 54 Assignment of voltage-gated potassium channel blocking activity to kappa-KTx1.3, a non-toxic homologue of kappa-hefutoxin-1, from Heterometrus spinifer venom. Biochem Pharmacol. 2005 Feb 15;69(4):669-78. doi: 10.1016/j.bcp.2004.10.018. Epub 2004 Dec 29.
Ref 55 Screening, large-scale production and structure-based classification of cystine-dense peptides. Nat Struct Mol Biol. 2018 Mar;25(3):270-278. doi: 10.1038/s41594-018-0033-9. Epub 2018 Feb 26.
Ref 56 A novel conotoxin inhibitor of Kv1.6 channel and nAChR subtypes defines a new superfamily of conotoxins. Biochemistry. 2006 Jul 11;45(27):8331-40. doi: 10.1021/bi060263r.
Ref 57 Engineered specific and high-affinity inhibitor for a subtype of inward-rectifier K+ channels. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10774-8. doi: 10.1073/pnas.0802850105. Epub 2008 Jul 31.
Ref 58 Mechanisms Underlying the Inhibition of KV1.3 Channel by Scorpion Toxin ImKTX58. Mol Pharmacol. 2022 Sep;102(3):150-160. doi: 10.1124/molpharm.121.000480. Epub 2022 Jun 28.
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