Peptide Information

General Information of This Peptide
Peptide ID
BTDP008413
Peptide Name
Kunitz-type serine protease inhibitor homolog dendrotoxin K
Symonym
Venom basic protease inhibitor K
Species
Dendroaspis polylepis polylepis (Black mamba)
Uniprot Name
VKTHK_DENPO
Alphafold ID
P00981
3D Structure
Download
2D Sequence
3D Structure
Source
RSCB PDB: 1DTK
Sequence
SGHLLLLLGLLTLWAELTPVSGAAKYCKLPLRIGPCKRKIPSFYYKWKAKQCLPFDYSGC
GGNANRFKTIEECRRTCVG
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Sequence Length
79
Mass (Da)
8852
Signal Sequence
SGHLLLLLGLLTLWAELTPVSG
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Sequence Removed Signal Peptide
AAKYCKLPLRIGPCKRKIPSFYYKWKAKQCLPFDYSGCGGNANRFKTIEECRRTCVG
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Disulfide Bond
27-77;36-60;52-73
PDB ID
1DTK
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Kingdom: Metazoa
Phylum: Chordata
Class: Lepidosauria
Order: Squamata
Family: Elapidae
Genus: Dendroaspis
Species: Dendroaspis polylepis
Full List of Activity Data of This Peptide Toxin
                        Target Name Activity Data Type Activity Data Concentration Note Reference
 Target Info    Kv1.1 Dissociation constant
0.24 nM
 .
Blocker
 [1- 7]
 Target Info    Kv1.1-1.2 Dissociation constant
0.57 nM
 .
Blocker
 [1- 7]
 Target Info    Kv1.1-1.2 Dissociation constant
0.71 nM
 .
Blocker
 [1- 7]
 Target Info    Kv1 Inhibition constant
0.29 nM
 .
Blocker
 [1- 7]
 Target Info    Kv1.2 Inhibition constant
2 nM
 .
Blocker
 [1- 7]
 Target Info    Kv1.6 Inhibition rate .
1 μM
Blocker
 [3]
 Target Info    Kv1.2 Inhibition rate .
1 μM
Blocker
 [3]
 Target Info    Kv1.2 Inhibition rate .
1 μM
Blocker
 [3]
 Target Info    Kv1.6-1.2 Inhibition rate .
3 μM
Blocker
 [1- 7]
 Target Info    Kv1.2 Inhibition rate .
100 nM
Blocker
 [1- 7]
 Target Info    Kv1.1 Effective concentration 50
0.03 nM
 .
Blocker
 [5]
 Target Info    Kv1.1 Effective concentration 50
0.6 nM
 .
Blocker
 [1- 7]
 Target Info    Kv1.1 IC50
0.05 nM
 .
Blocker
 [1- 7]
 Target Info    Kv1.1-1.2 IC50
0.1 nM
 .
Blocker
 [1- 7]
 Target Info    Kv1.1-1.2 IC50
0.45 nM
 .
Blocker
 [1- 7]
 Target Info    Kv1 IC50
2.5 nM
 .
Blocker
 [1- 7]
 Target Info    Kv1.1-1.2 IC50
18.8 nM
 .
Blocker
 [1- 7]
References
Ref 1 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 2 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 3 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 4 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 5 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 6 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 7 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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