Peptide Information

General Information of This Peptide
Peptide ID
BTDP008687
Peptide Name
Potassium channel toxin alpha-KTx 6.2
Symonym
Maurotoxin
Species
Scorpio palmatus (Israeli golden scorpion) (Scorpio maurus palmatus)
Uniprot Name
KAX62_SCOPA
Alphafold ID
P80719
3D Structure
Download
2D Sequence
3D Structure
Source
RSCB PDB: 1TXM
Sequence
VSCTGSKDCYAPCRKQTGCPNAKCINKSCKCYGC
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Sequence Length
34
Mass (Da)
3621
Sequence Removed Signal Peptide
VSCTGSKDCYAPCRKQTGCPNAKCINKSCKCYGC
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Disulfide Bond
3-24;9-29;13-19;31-34
PDB ID
1TXM , 1WPD , 1WT7
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Kingdom: Metazoa
Phylum: Arthropoda
Class: Arachnida
Order: Scorpiones
Family: Scorpionidae
Genus: Scorpio
Species: Scorpio palmatus
Full List of Activity Data of This Peptide Toxin
                        Target Name Activity Data Type Activity Data Concentration Note Reference
 Target Info    KCa2.2 Dissociation constant
1 μM
 .
Blocker
 [1]
 Target Info    KCa1.1 Inhibition rate .
1 μM
Blocker
 [2]
 Target Info    KCa2.3 Inhibition rate .
1 μM
Blocker
 [1]
 Target Info    Kv1.2 IC50
0.12 - 0.8 nM
 .
Blocker
 [1- 13]
 Target Info    Kv1 IC50
0.2 nM
 .
Blocker
 [1- 13]
 Target Info    Kv1.2 IC50
0.8 nM
 .
Blocker
 [1- 13]
 Target Info    KCa3.1 IC50
1 nM
 .
Blocker
 [2]
 Target Info    KCa3.1 IC50
1.2 - 2 nM
 .
Blocker
 [1- 13]
 Target Info    Shaker B potassium channel IC50
2.39 - 80 nM
 .
Blocker
 [1- 13]
 Target Info    Shaker IC50
2.4 nM
 .
Blocker
 [8]
 Target Info    KCa2 IC50
5 nM
 .
Blocker
 [1- 13]
 Target Info    Kv1.1 IC50
37 - 45 nM
 .
Blocker
 [1- 13]
 Target Info    Kv1 IC50
45 nM
 .
Blocker
 [1- 13]
 Target Info    Kv1.3 IC50
150 - 180 nM
 .
Blocker
 [1- 13]
 Target Info    Kv1.3 IC50
180 nM
 .
Blocker
 [1- 13]
References
Ref 1 Design and characterization of a highly selective peptide inhibitor of the small conductance calcium-activated K+ channel, SkCa2. J Biol Chem. 2001 Nov 16;276(46):43145-51. doi: 10.1074/jbc.M106981200. Epub 2001 Aug 29.
Ref 2 Maurotoxin: a potent inhibitor of intermediate conductance Ca2+-activated potassium channels. Mol Pharmacol. 2003 Feb;63(2):409-18. doi: 10.1124/mol.63.2.409.
Ref 3 Chemical synthesis and characterization of maurotoxin, a short scorpion toxin with four disulfide bridges that acts on K+ channels. Eur J Biochem. 1996 Dec 15;242(3):491-8. doi: 10.1111/j.1432-1033.1996.0491r.x.
Ref 4 Maurotoxin, a four disulfide bridge toxin from Scorpio maurus venom: purification, structure and action on potassium channels. FEBS Lett. 1997 Apr 14;406(3):284-90. doi: 10.1016/s0014-5793(97)00285-8.
Ref 5 Maurotoxin, a four disulfide bridges scorpion toxin acting on K+ channels. Toxicon. 1998 Nov;36(11):1609-11. doi: 10.1016/s0041-0101(98)00153-6.
Ref 6 Mechanisms of maurotoxin action on Shaker potassium channels. Biophys J. 2000 Aug;79(2):776-87. doi: 10.1016/S0006-3495(00)76335-1.
Ref 7 Maurotoxin versus Pi1/HsTx1 scorpion toxins. Toward new insights in the understanding of their distinct disulfide bridge patterns. J Biol Chem. 2000 Dec 15;275(50):39394-402. doi: 10.1074/jbc.M006810200.
Ref 8 Effect of maurotoxin, a four disulfide-bridged toxin from the chactoid scorpion Scorpio maurus, on Shaker K+ channels. J Pept Res. 2000 Jun;55(6):419-27. doi: 10.1034/j.1399-3011.2000.00715.x.
Ref 9 Evidence for domain-specific recognition of SK and Kv channels by MTX and HsTx1 scorpion toxins. J Biol Chem. 2004 Dec 31;279(53):55690-6. doi: 10.1074/jbc.M410055200. Epub 2004 Oct 21.
Ref 10 Chemical synthesis and 1H-NMR 3D structure determination of AgTx2-MTX chimera, a new potential blocker for Kv1.2 channel, derived from MTX and AgTx2 scorpion toxins. Protein Sci. 2008 Jan;17(1):107-18. doi: 10.1110/ps.073122908. Epub 2007 Nov 27.
Ref 11 Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels. Proteins. 1997 Nov;29(3):321-33.
Ref 12 Structural and functional consequences of the presence of a fourth disulfide bridge in the scorpion short toxins: solution structure of the potassium channel inhibitor HsTX1. Protein Sci. 1999 Dec;8(12):2672-85. doi: 10.1110/ps.8.12.2672.
Ref 13 Increasing the molecular contacts between maurotoxin and Kv1.2 channel augments ligand affinity. Proteins. 2005 Aug 15;60(3):401-11. doi: 10.1002/prot.20509.
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