Target Information

General Information of This Target
Target ID
BTDT10312
Target Name
para/tipE
Target Bioclass
Transporter and channel
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N.A.
Species: Insect
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Alpha-toxin OD1 Effective concentration 50
80 nM
 [1], [2], [3], [4]
 Toxin Info    Mu-theraphotoxin-Hhn2b 1 IC50
4.3 μM
 [5], [6], [7], [8]
 Toxin Info    Mu-theraphotoxin-Hhn2b 2 IC50
4.3 μM
 [5], [6], [7], [8]
 Toxin Info    Mu-theraphotoxin-Hhn2b 3 IC50
4.3 μM
 [5], [6], [7], [8]
References
Ref 1 OD1, the first toxin isolated from the venom of the scorpion Odonthobuthus doriae active on voltage-gated Na+ channels. FEBS Lett. 2005 Aug 1;579(19):4181-6. doi: 10.1016/j.febslet.2005.06.052.
Ref 2 Potent modulation of the voltage-gated sodium channel Nav1.7 by OD1, a toxin from the scorpion Odonthobuthus doriae. Mol Pharmacol. 2006 Jul;70(1):405-14. doi: 10.1124/mol.106.022970. Epub 2006 Apr 26.
Ref 3 Analgesic Effects of GpTx-1, PF-04856264 and CNV1014802 in a Mouse Model of NaV1.7-Mediated Pain. Toxins (Basel). 2016 Mar 17;8(3):78. doi: 10.3390/toxins8030078.
Ref 4 Chemical engineering and structural and pharmacological characterization of the -scorpion toxin OD1. ACS Chem Biol. 2013;8(6):1215-22. doi: 10.1021/cb400012k. Epub 2013 Apr 3.
Ref 5 Molecular diversification of peptide toxins from the tarantula Haplopelma hainanum (Ornithoctonus hainana) venom based on transcriptomic, peptidomic, and genomic analyses. J Proteome Res. 2010 May 7;9(5):2550-64. doi: 10.1021/pr1000016.
Ref 6 Purification and characterization of Hainantoxin-V, a tetrodotoxin-sensitive sodium channel inhibitor from the venom of the spider Selenocosmia hainana. Toxicon. 2003 May;41(6):643-50. doi: 10.1016/s0041-0101(02)00280-5.
Ref 7 Function and solution structure of hainantoxin-I, a novel insect sodium channel inhibitor from the Chinese bird spider Selenocosmia hainana. FEBS Lett. 2003 Dec 18;555(3):616-22. doi: 10.1016/s0014-5793(03)01303-6.
Ref 8 Rational Engineering Defines a Molecular Switch That Is Essential for Activity of Spider-Venom Peptides against the Analgesics Target NaV1.7. Mol Pharmacol. 2015 Dec;88(6):1002-10. doi: 10.1124/mol.115.100784. Epub 2015 Oct 1.
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