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Scorpion toxins are proteins found in the venom of scorpions. Their toxic effect may be mammal or insect specific, and acts by binding to sodium channels, inhibiting the inactivation of activated channels and blocking neuronal transmission. 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 (). This group of proteins is now used in the creation of insecticides, vaccines, and protein engineering scaffolds. == Structure == The complete covalent structure of several such toxins has been deduced: They comprise around 66 amino acid residues forming a three stranded anti-parallel beta sheet over which lies an alpha helix of approximately three turns. Four disulfide bridges cross-link the structure of the long-chain toxins whereas the short toxins contain only three. BmKAEP, an anti-epilepsy peptide isolated from the venom of the Manchurian scorpion, shows similarity to both scorpion neurotoxins and anti-insect toxins. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「scorpion toxin」の詳細全文を読む スポンサード リンク
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