Target Information

General Information of This Target
Target ID
BTDT10004
Target Name
A-type voltage-gated potassium channel
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    Potassium channel toxin alpha-KTx 15.3 Inhibition constant
131 nM
 [1- 5]
 Toxin Info    Potassium channel toxin alpha-KTx 15.6 IC50
190 nM
 [2- 11]
References
Ref 1 Expanding the scorpion toxin alpha-KTX 15 family with AmmTX3 from Androctonus mauretanicus. Eur J Biochem. 2002 Dec;269(24):6037-41. doi: 10.1046/j.1432-1033.2002.03294.x.
Ref 2 A common "hot spot" confers hERG blockade activity to alpha-scorpion toxins affecting K+ channels. Biochem Pharmacol. 2008 Sep 15;76(6):805-15. doi: 10.1016/j.bcp.2008.07.008. Epub 2008 Jul 18.
Ref 3 Dipeptidyl-peptidase-like-proteins confer high sensitivity to the scorpion toxin AmmTX3 to Kv4-mediated A-type K+ channels. J Physiol. 2013 May 15;591(10):2419-27. doi: 10.1113/jphysiol.2012.248831. Epub 2013 Feb 25.
Ref 4 Kv4 channel blockade reduces motor and neuropsychiatric symptoms in rodent models of Parkinson's disease. Behav Pharmacol. 2015 Feb;26(1-2):91-100. doi: 10.1097/FBP.0000000000000107.
Ref 5 Synthesis by native chemical ligation and characterization of the scorpion toxin AmmTx3. Bioorg Med Chem. 2019 Jan 1;27(1):247-253. doi: 10.1016/j.bmc.2018.12.009. Epub 2018 Dec 6.
Ref 6 Molecular cloning and nucleotide sequence analysis of genes from a cDNA library of the scorpion Tityus discrepans. Biochimie. 2009 Aug;91(8):1010-9. doi: 10.1016/j.biochi.2009.05.005. Epub 2009 May 24.
Ref 7 Discrepin, a new peptide of the sub-family alpha-ktx15, isolated from the scorpion Tityus discrepans irreversibly blocks K+ -channels (IA currents) of cerebellum granular cells. Arch Biochem Biophys. 2004 Oct 15;430(2):256-63. doi: 10.1016/j.abb.2004.07.010.
Ref 8 Proteomic analysis of Tityus discrepans scorpion venom and amino acid sequence of novel toxins. Proteomics. 2006 Jun;6(12):3718-27. doi: 10.1002/pmic.200500525.
Ref 9 A positive charge at the N-terminal segment of Discrepin increases the blocking effect of K+ channels responsible for the IA currents in cerebellum granular cells. Biochim Biophys Acta. 2008 Apr;1780(4):750-5. doi: 10.1016/j.bbagen.2008.01.012. Epub 2008 Jan 30.
Ref 10 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 11 Solution structure of discrepin, a new K+-channel blocking peptide from the alpha-KTx15 subfamily. Biochemistry. 2006 Feb 14;45(6):1795-804. doi: 10.1021/bi0519248.
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