Peptide Information

General Information of This Peptide
Peptide ID
BTDP008412
Peptide Name
Kunitz-type serine protease inhibitor homolog dendrotoxin I
Symonym
Dendrotoxin-1; Venom basic protease inhibitor 1
Species
Dendroaspis polylepis polylepis (Black mamba)
Uniprot Name
VKTH1_DENPO
Alphafold ID
P00979
3D Structure
Download
2D Sequence
3D Structure
Source
RSCB PDB: 1DEM
Sequence
QPLRKLCILHRNPGRCYQKIPAFYYNQKKKQCEGFTWSGCGGNSNRFKTIEECRRTCIRK
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Sequence Length
60
Mass (Da)
7155
Sequence Removed Signal Peptide
QPLRKLCILHRNPGRCYQKIPAFYYNQKKKQCEGFTWSGCGGNSNRFKTIEECRRTCIRK
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Disulfide Bond
7-57;16-40;32-53
PDB ID
1DEM , 1DEN
        Click to Show/Hide the Complete Species Lineage
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    Kv1.3 Inhibition rate .
100 nM
Blocker
 [1]
 Target Info    Kir3.1/3.4 Inhibition rate .
1 μM
Blocker
 [2- 6]
 Target Info    Kv1.4 Inhibition rate .
1 μM
Blocker
 [7]
 Target Info    Kv4.2 Inhibition rate .
300 nM
Blocker
 [8]
 Target Info    Kv1.6 Inhibition rate
26 %
10 nM
Blocker
 [4]
 Target Info    Kv1.1 Effective concentration 50
7.4 nM
 .
Blocker
 [9]
 Target Info    Kv1.1 IC50
0.13 - 50 nM
 .
Blocker
 [2- 10]
 Target Info    Kv1.2 IC50
0.13 - 50 nM
 .
Blocker
 [2- 10]
 Target Info    Kv1.6 IC50
0.13 - 50 nM
 .
Blocker
 [2- 10]
 Target Info    Kv1.2 IC50
0.13 nM
 .
Blocker
 [11]
 Target Info    Kv1.1 IC50
3.1 nM
 .
Blocker
 [11]
 Target Info    Kv1.3 IC50
4.533 μM
 .
Blocker
 [12]
References
Ref 1 A rapidly activating and slowly inactivating potassium channel cloned from human heart. Functional analysis after stable mammalian cell culture expression. J Gen Physiol. 1993 Apr;101(4):513-43. doi: 10.1085/jgp.101.4.513.
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 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 5 Sequence-specific 1H-NMR assignment and secondary structure of black mamba dendrotoxin I, a highly selective blocker of voltage-gated potassium channels. Eur J Biochem. 1993 Feb 1;211(3):813-20. doi: 10.1111/j.1432-1033.1993.tb17613.x.
Ref 6 Proteinase inhibitor homologues as potassium channel blockers. Nat Struct Biol. 1994 Apr;1(4):246-50. doi: 10.1038/nsb0494-246.
Ref 7 Toxin and subunit specificity of blocking affinity of three peptide toxins for heteromultimeric, voltage-gated potassium channels expressed in Xenopus oocytes. J Pharmacol Exp Ther. 1998 Jun;285(3):1051-60.
Ref 8 Functional characterization of RK5, a voltage-gated K+ channel cloned from the rat cardiovascular system. FEBS Lett. 1991 Dec 16;295(1-3):211-3. doi: 10.1016/0014-5793(91)81420-d.
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 Protease inhibitors as snake venom toxins. Nat New Biol. 1973 May 16;243(124):88-9.
Ref 11 Properties of voltage-gated K+ currents expressed in Xenopus oocytes by mKv1.1, mKv1.2 and their heteromultimers as revealed by mutagenesis of the dendrotoxin-binding site in mKv1.1. Pflugers Arch. 1994 Oct;428(3-4):382-90. doi: 10.1007/BF00724522.
Ref 12 Both N- and C-terminal regions contribute to the assembly and functional expression of homo- and heteromultimeric voltage-gated K+ channels. J Neurosci. 1994 Mar;14(3 Pt 1):1385-93. doi: 10.1523/JNEUROSCI.14-03-01385.1994.
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