Target Information

General Information of This Target
Target ID
BTDT10243
Target Name
Shaker IR potassium channel
Target Bioclass
Transporter and channel
Taxonomy ID
7227
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Kingdom: Metazoa
Phylum: Arthropoda
Class: Insecta
Order: Diptera
Family: Drosophilidae
Genus: Drosophila
Species: Drosophila melanogaster
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Conotoxin im23a Effect . [1]
 Toxin Info    Conotoxin im23b Effect . [1], [2]
 Toxin Info    Potassium channel toxin alpha-KTx 31.1 Inhibition rate
100 %
 [3]
 Toxin Info    Kappa-conotoxin PVIIA IC50
57 - 80 nM
 [4- 15]
 Toxin Info    Kappa-actitoxin-Bcs4a IC50
94.25 nM
 [16]
 Toxin Info    PI-stichotoxin-Hcr2g IC50
114.9 nM
 [17], [18], [19]
 Toxin Info    PI-stichotoxin-Hcr2f IC50
433.1 nM
 [17], [18], [19]
References
Ref 1 A helical conotoxin from Conus imperialis has a novel cysteine framework and defines a new superfamily. J Biol Chem. 2012 Apr 27;287(18):14973-83. doi: 10.1074/jbc.M111.334615. Epub 2012 Mar 7.
Ref 2 Transcriptomic-Proteomic Correlation in the Predation-Evoked Venom of the Cone Snail, Conus imperialis. Mar Drugs. 2019 Mar 19;17(3):177. doi: 10.3390/md17030177.
Ref 3 Kbot55, purified from Buthus occitanus tunetanus venom, represents the first member of a novel -KTx subfamily. Peptides. 2016 Jun;80:4-8. doi: 10.1016/j.peptides.2015.05.015. Epub 2015 Jun 14.
Ref 4 kappa-Conotoxin PVIIA is a peptide inhibiting the shaker K+ channel. J Biol Chem. 1998 Jan 2;273(1):33-8. doi: 10.1074/jbc.273.1.33.
Ref 5 Strategy for rapid immobilization of prey by a fish-hunting marine snail. Nature. 1996 May 9;381(6578):148-51. doi: 10.1038/381148a0.
Ref 6 The block of Shaker K+ channels by kappa-conotoxin PVIIA is state dependent. J Gen Physiol. 1999 Jul;114(1):125-40. doi: 10.1085/jgp.114.1.125.
Ref 7 Single amino acid substitutions in kappa-conotoxin PVIIA disrupt interaction with the shaker K+ channel. J Biol Chem. 2000 Aug 11;275(32):24639-44. doi: 10.1074/jbc.C900990199.
Ref 8 Molecular simulation of the interaction of kappa-conotoxin-PVIIA with the Shaker potassium channel pore. Eur Biophys J. 2001 Dec;30(7):528-36. doi: 10.1007/s00249-001-0189-8.
Ref 9 Inhibition of single Shaker K channels by kappa-conotoxin-PVIIA. Biophys J. 2002 Jun;82(6):3003-11. doi: 10.1016/S0006-3495(02)75641-5.
Ref 10 Electrostatic recognition and induced fit in the kappa-PVIIA toxin binding to Shaker potassium channel. J Am Chem Soc. 2005 May 11;127(18):6836-49. doi: 10.1021/ja042641q.
Ref 11 Postischemic administration of CGX-1051, a peptide from cone snail venom, reduces infarct size in both rat and dog models of myocardial ischemia and reperfusion. J Cardiovasc Pharmacol. 2005 Aug;46(2):141-6. doi: 10.1097/01.fjc.0000167015.84715.27.
Ref 12 Why the Drosophila Shaker K+ channel is not a good model for ligand binding to voltage-gated Kv1 channels. Biochemistry. 2013 Mar 5;52(9):1631-40. doi: 10.1021/bi301257p. Epub 2013 Feb 20.
Ref 13 Efficient enzymatic cyclization of an inhibitory cystine knot-containing peptide. Biotechnol Bioeng. 2016 Oct;113(10):2202-12. doi: 10.1002/bit.25993. Epub 2016 Aug 9.
Ref 14 Solution structure and proposed binding mechanism of a novel potassium channel toxin kappa-conotoxin PVIIA. Structure. 1997 Dec 15;5(12):1585-97. doi: 10.1016/s0969-2126(97)00307-9.
Ref 15 Three-dimensional structure of kappa-conotoxin PVIIA, a novel potassium channel-blocking toxin from cone snails. Biochemistry. 1998 Apr 21;37(16):5407-16. doi: 10.1021/bi9730341.
Ref 16 BcsTx3 is a founder of a novel sea anemone toxin family of potassium channel blocker. FEBS J. 2013 Oct;280(19):4839-52. doi: 10.1111/febs.12456. Epub 2013 Aug 23.
Ref 17 New Kunitz-Type HCRG Polypeptides from the Sea Anemone Heteractis crispa. Mar Drugs. 2015 Sep 24;13(10):6038-63. doi: 10.3390/md13106038.
Ref 18 Kunitz-Type Peptides from the Sea Anemone Heteractis crispa Demonstrate Potassium Channel Blocking and Anti-Inflammatory Activities. Biomedicines. 2020 Nov 4;8(11):473. doi: 10.3390/biomedicines8110473.
Ref 19 Sea Anemone Kunitz-Type Peptides Demonstrate Neuroprotective Activity in the 6-Hydroxydopamine Induced Neurotoxicity Model. Biomedicines. 2021 Mar 10;9(3):283. doi: 10.3390/biomedicines9030283.
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