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Scorpion toxins are proteins, which may be mammal or insect specific, bind to sodium channels, inhibiting the inactivation of activated channels and blocking neuronal transmission. The complete covalent structure of the toxins has been deduced: it comprises around 66 amino acid residues and is cross- linked by 4 disulphide bridges. An anti-epilepsy peptide isolated from scorpion venom shows similarity to both scorpion neurotoxins and anti-insect toxins.
Additional recommended knowledge
This family includes related short- and long-chain scorpion toxins. It also contains a group of proteinase inhibitors from 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 (IPR001254).
This family contains both neurotoxins and plant defensins. The mustard trypsin inhibitor, MTI-2, is plant defensin. It is a potent inhibitor of trypsin with no activity towards chymotrypsin. MTI-2 is toxic for Lepidopteran insects, but has low activity against aphids. Brazzein is plant defensin-like protein. It is pH-stable, heat-stable and intensely sweet protein 
This article includes text from the public domain Pfam and InterPro IPR002061
Categories: Protein domains | Peripheral membrane proteins
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Scorpion_toxin". A list of authors is available in Wikipedia.|