Target Information

General Information of This Target
Target ID
BTDT10178
Target Name
Potassium voltage-gated channel subfamily A member 1;Potassium voltage-gated channel subfamily A 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    Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin Dissociation constant
0.34 nM
 [1], [2], [3], [4]
 Toxin Info    Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin Dissociation constant
0.5 nM
 [1], [2], [3], [4]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin K Dissociation constant
0.57 nM
 [5- 11]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin K Dissociation constant
0.71 nM
 [5- 11]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin K IC50
0.1 nM
 [5- 11]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin K IC50
0.45 nM
 [5- 11]
 Toxin Info    Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin IC50
8 nM
 [1], [2], [3], [4]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin K IC50
18.8 nM
 [5- 11]
References
Ref 1 Snake venoms. The amino acid sequences of two proteinase inhibitor homologues from Dendroaspis angusticeps venom. Hoppe Seylers Z Physiol Chem. 1980 May;361(5):661-74. doi: 10.1515/bchm2.1980.361.1.661.
Ref 2 Twenty years of dendrotoxins. Toxicon. 2001 Jan;39(1):15-26. doi: 10.1016/s0041-0101(00)00162-8.
Ref 3 Protease inhibitors from marine venomous animals and their counterparts in terrestrial venomous animals. Mar Drugs. 2013 Jun 14;11(6):2069-112. doi: 10.3390/md11062069.
Ref 4 Crystal structure of alpha-dendrotoxin from the green mamba venom and its comparison with the structure of bovine pancreatic trypsin inhibitor. J Mol Biol. 1992 Apr 5;224(3):671-83. doi: 10.1016/0022-2836(92)90552-u.
Ref 5 Cloning and functional expression of dendrotoxin K from black mamba, a K+ channel blocker. Biochemistry. 1993 Jun 1;32(21):5692-7. doi: 10.1021/bi00072a026.
Ref 6 Snake venom toxins. The amino acid sequence of toxin Vi2, a homologue of pancreatic trypsin inhibitor, from Dendroaspis polylepis polylepis (black mamba) venom. Biochim Biophys Acta. 1977 Apr 25;491(2):361-9. doi: 10.1016/0005-2795(77)90279-3.
Ref 7 Novel effects of dendrotoxin homologues on subtypes of mammalian Kv1 potassium channels expressed in Xenopus oocytes. FEBS Lett. 1996 Mar 25;383(1-2):26-30. doi: 10.1016/0014-5793(96)00211-6.
Ref 8 Site-directed mutagenesis of dendrotoxin K reveals amino acids critical for its interaction with neuronal K+ channels. Biochemistry. 1997 Jun 24;36(25):7690-6. doi: 10.1021/bi963105g.
Ref 9 The relative potencies of dendrotoxins as blockers of the cloned voltage-gated K+ channel, mKv1.1 (MK-1), when stably expressed in Chinese hamster ovary cells. Br J Pharmacol. 1997 Mar;120(6):1029-34. doi: 10.1038/sj.bjp.0701004.
Ref 10 Identification of residues in dendrotoxin K responsible for its discrimination between neuronal K+ channels containing Kv1.1 and 1.2 alpha subunits. Eur J Biochem. 1999 Jul;263(1):222-9. doi: 10.1046/j.1432-1327.1999.00494.x.
Ref 11 Nuclear magnetic resonance solution structure of dendrotoxin K from the venom of Dendroaspis polylepis polylepis. J Mol Biol. 1993 Dec 5;234(3):735-50. doi: 10.1006/jmbi.1993.1623.
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