[1] The protein is also referred to as kappa-Buthitoxin-Im1a, in line with the rational nomenclature system used for toxins produced by venomous species.
[1][2] ImKTX58 is derived from the venom secreted by the glands of Isometrus maculatus (also known as the lesser brown scorpion) which belongs to the Buthidae family.
[1] It features an α-helix at the N-terminus and β-sheet framework at the C-terminus reinforced by cysteine residues and three disulfide bridges, which contribute to its stability.
[1] ImKTX58 exerts a partially reversible pore-blocking effect by forming a protein complex with Kv1.3 channels.
[1] This pore blockage leads to increased cellular excitability, ultimately disrupting the regulation of the cell membrane potential.