page_title: Maurotoxin
hierarchical_section_title: Maurotoxin
caption_attribution_description: A protein NMR structure of the four-disulfide-bridge scorpion toxin maurotoxin, which inhibits potassium ion channels. The protein backbone is shown in red, the alpha carbons of the eight cysteine residues are shown in green, and the disulfide bridges themselves are shown in yellow. The maurotoxin disulfide bridge connectivity is uncommon among scorpion toxins. Multiple structures are shown to reflect the natural fluctuations in native-state protein structure in solution.
context_page_description: Maurotoxin 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.
context_section_description: 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.
caption: 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.
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