AA sequence: Val-Ser-Cys3-Thr-Gly-Ser-Lys-Asp-Cys9-Tyr-Ala-Pro-Cys13-Arg-Lys-Gln-Thr-Gly-Cys19-Pro-Asn-Ala-Lys-Cys24-Ile-Asn-Lys-Ser-Cys29-Lys-Cys31-Tyr-Gly-Cys34-NH2
Disulfide bonds: Cys3-Cys24, Cys9-Cys29, Cys13-Cys19 and Cys31 -Cys34
Length (aa): 34
Formula: C145H231N45O47S8
Molecular Weight: 3612.55 Da
Appearance: White lyophilized solid
Solubility: water or saline buffer
CAS number: not available
Source: Synthetic
Purity rate: > 95 %
Maurotoxin
Maurotoxin Kv and SK channels blocker
Maurotoxin is a component of the venom of Scorpio maurus palmatus. Maurotoxin is a member of the α-KTx6.2 scorpion toxin family. It blocks voltage-gated potassium channels (KV1.1/KCNA1, KV1.2/KCNA2, and KV1.3/KCNA3) and inhibits apamin-sensitive small conductance calcium-activated channels (SK channels), particularly KCa3.1 (IKca1, SK4). The blockage of Kv1.2 occurs with high affinity.
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Analysis of the interacting surface of maurotoxin with the voltage-gated Shaker B K(+) channel
Effect of maurotoxin, a four disulfide-bridged toxin from the chactoid scorpion Scorpio maurus, on Shaker K+ channels
Maurotoxin, a four disulfide bridges scorpion toxin acting on K+ channels
Rochat, H., et al. (1998) Maurotoxin, a four disulfide bridges scorpion toxin acting on K+ channels, Toxicon. PMID: 9792177
Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels
Maurotoxin (MTX), purified from the scorpionid Scorpio maurus is a potent ligand for potassium channels. It shows a broad specificity as being active on Kv1.1 (Kd = 37 nM), Kv1.2 (Kd = 0.8 nM), Kv1.3 (Kd = 150 nM) voltage-gated potassium channels, as well as on small-conductance calcium-activated potassium channels. It has a unique disulfide pairing among the scorpion toxins family. The solution structure of MTX has been determined by 2D-NMR techniques, which led to the full description of its 3D conformation: a bended helix from residues 6 to 16 connected by a loop to a two-stranded antiparallel beta sheet (residues 23 to 26 and 28 to 31). The interaction of MTX with the pore region of the Kv1.2 potassium channel has been modeled according to their charge anisotropy. The structure of MTX is similar to other short scorpion toxins despite its peculiar disulfide pairing. Its interaction with the Kv1.2 channel involves a dipole moment, which guides and orients the toxin onto the pore, toward the binding site, and which thus is responsible for the specificity.
Blanc, E., et al. (1997) Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels, Proteins. PMID: 9365987