Target Information

General Information of This Target
Target ID
BTDT10202
Target Name
Potassium voltage-gated channel subfamily C member 2
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    Delta/kappa-actitoxin-Avd4a Inhibition rate . [1- 6]
 Toxin Info    Kappa-theraphotoxin-Ps1a Inhibition rate . [7], [8], [9]
 Toxin Info    Kappa-theraphotoxin-Ps1b Inhibition rate . [7]
 Toxin Info    Delta/kappa-actitoxin-Avd4a Inhibition rate
48 %
 [1- 6]
 Toxin Info    DeltaKappa-actitoxin-Avd4b Inhibition rate
50 %
 [1], [2], [4]
References
Ref 1 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 2 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 3 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 4 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 5 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 6 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 7 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 8 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 9 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.
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