<unk> -1 is a 4 kDa peptide consisting of 36 amino acids with six positively charged residues and six cysteines, which forms three disulfide bridges. The primary amino acid sequence of<unk> -1 is: H-Arg-Pro-Thr-Asp-Ile-Lys-Cys-Ser-Glu-Ser-Tyr-Gln-Cys-Phe-Pro-Val-Cys-Lys-Ser-Arg-Phe-Gly-Lys-Thr-Asn-Gly-Arg-Cys-Val-Asn-Gly-Phe-Cys-Asp-Cys-Phe-OH. Its tertiary structure consists of an alpha-helix and three beta-strands, arranged in a strongly twisted antiparallel beta sheet, compactly fold up. The helix is confined by two ‘caps’ that have also been described in other short scorpion toxins.<unk> -1 shows structural homology to the family of scorpion venom potassium channel blockers, the α-KTx family. Despite the similarities between<unk> -1 and these scorpion toxins,<unk> -1 belongs to a new subfamily of scorpion K1 channel blocking peptides. The differences between the subfamilies are in the COOH-terminal part: the newly described family of toxins,<unk> -1 included, contains Arg<unk> 7, Val 29 and Phe32, while the older one Lys, Met and Lys.
BeKm-1 toxin
Chlorotoxin
Toxic shock syndrome toxin
Maitotoxin
Hemotoxin
Kurtoxin
Psalmotoxin
Vanillotoxin