Scorpion toxin
Scorpion toxins are proteins found in the venom of scorpions. Their toxic effect may be mammal- or insect-specific and acts by binding with varying degrees of specificity to members of the Voltage-gated ion channel superfamily; specifically, voltage-gated sodium channels, voltage-gated potassium channels, and Transient Receptor Potential (TRP) channels. The result of this action is to activate or inhibit the action of these channels in the nervous and cardiac organ systems. For instance, α-scorpion toxins MeuNaTxα-12 and MeuNaTxα-13 from Mesobuthus eupeus are neurotoxins that target voltage-gated Na+ channels (Navs), inhibiting fast inactivation. In vivo assays of MeuNaTxα-12 and MeuNaTxα-13 effects on mammalian and insect Navs show differential potency. These recombinants (MeuNaTxα-12 and MeuNaTxα-13) exhibit their preferential affinity for mammalian and insect Na+ channels at the α-like toxins' active site, site 3, in order to inactivate the cell membrane depolarization faster[6]. The varying sensitivity of different Navs to MeuNaTxα-12 and MeuNaTxα-13 may be dependent on the substitution of a conserved Valine residue for a Phenylalanine residue at position 1630 of the LD4:S3-S4 subunit or due to various changes in residues in the LD4:S5-S6 subunit of the Navs. Ultimately, these actions can serve the purpose of warding off predators by causing pain (e.g., through the activation of sodium channels or TRP channels in sensory neurons) or to subdue predators (e.g., in the case of inhibition of cardiac ion channels).
| Scorpion long-chain toxin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Crystal structure of toxin II from the scorpion Androctonus australis Hector. | |||||||||
| Identifiers | |||||||||
| Symbol | Toxin_3 | ||||||||
| Pfam | PF00537 | ||||||||
| InterPro | IPR002061 | ||||||||
| SCOP2 | 2sn3 / SCOPe / SUPFAM | ||||||||
| TCDB | 8.B.1 | ||||||||
| OPM superfamily | 58 | ||||||||
| OPM protein | 1djt | ||||||||
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| Scorpion short toxin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Toxin_2 | ||||||||
| Pfam | PF00451 | ||||||||
| Pfam clan | CL0054 | ||||||||
| InterPro | IPR001947 | ||||||||
| PROSITE | PDOC00875 | ||||||||
| TCDB | 8.B.2 | ||||||||
| OPM superfamily | 58 | ||||||||
| OPM protein | 1ne5 | ||||||||
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The family includes related short- and long-chain scorpion toxins. It also contains a group of proteinase inhibitors from the plants Arabidopsis thaliana and Brassica spp.
The Brassica napus (oil seed rape) and Sinapis alba (white mustard) inhibitors, inhibit the catalytic activity of bovine beta-trypsin and bovine alpha-chymotrypsin, which belong to MEROPS peptidase family S1 (InterPro: IPR001254).
This group of proteins is now used in the creation of insecticides, vaccines, and protein engineering scaffolds.