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The protein NMR structure of maurotoxin, illustrating the fluctuations in the protein's native state in solution. The protein backbone is shown in red, the alpha carbons of the eight cysteine residues in green, and the disulfide bridges in yellow. Compare the disulfide bond connectivity to HsTx1 below.

The protein NMR structure of HsTx1, a scorpion toxin with a canonical disulfide bond connectivity.

Maurotoxin (abbreviated MTX) is a peptide toxin from the venom of the Tunisian chactoid scorpion Scorpio maurus palmatus, from which it was first isolated and from which the chemical gets its name. It acts by blocking several types of voltage-gated potassium channel.