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Maurotoxin: Difference between revisions

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Importing Wikidata short description: "Toxin in scorpions"
 
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{{Short description|Toxin in scorpions}}
{{Inline citations|date=June 2019}}[[Image:Maurotoxin 1txm.png|thumb|right|250px|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 carbon]]s of the eight [[cysteine]] residues in green, and the [[disulfide bridge]]s in yellow. Compare the disulfide bond connectivity to HsTx1 below.]]
[[Image:Hstx1_1quz.png|thumb|right|250px|The [[protein NMR]] structure of HsTx1, a scorpion toxin with a canonical disulfide bond connectivity.]]
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== Chemistry ==
Maurotoxin is a peptide of 34 [[amino acid]]s (sequence VSCTGSKDCYAPCRKQTGCPNAKCINKSCKCYGC) cross-linked by four [[disulfide bridge]]s (Cys3-Cys24, Cys9-Cys29, Cys13-Cys19, Cys31-Cys34), with an atypical pattern of organization compared with other scorpion toxins; this unusual pairing of [[cysteine]] residues may be mediated by the presence of adjacent [[proline]]s. The peptide contains an [[alpha helix]] linked by two disulfide bridges to a two-stranded antiparallel [[beta sheet]].
 
== Target ==
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== References ==
 
# Carlier, E., ''et al.'', Effect of maurotoxin, a four disulfide-bridged toxin from the chactoid scorpion Scorpio maurus, on Shaker K+ channels. J Pept Res, 2000. 55(6): p. 419-27419–27.
# Castle, N.A., ''et al.'', Maurotoxin: a potent inhibitor of intermediate conductance Ca2+-activated potassium channels. Mol Pharmacol, 2003. 63(2): p. 409-18409–18.
# Fu, W., ''et al.'', Brownian dynamics simulations of the recognition of the scorpion toxin maurotoxin with the voltage-gated potassium ion channels. Biophys J, 2002. 83(5): p. 2370-852370–85.
# Jensen, B.S., ''et al.'', The Ca2+-activated K+ channel of intermediate conductance:a possible target for immune suppression. Expert Opin Ther Targets, 2002. 6(6): p. 623-36623–36.
# Kharrat, R., ''et al.'', Chemical synthesis and characterization of maurotoxin, a short scorpion toxin with four disulfide bridges that acts on K+ channels. Eur J Biochem, 1996. 242(3): p. 491-8491–8.
# M'Barek, S., ''et al.'', A maurotoxin with constrained standard disulfide bridging: innovative strategy of chemical synthesis, pharmacology, and docking on K+ channels. J Biol Chem, 2003. 278(33): p. 31095-10431095–104.
# Rochat, H., ''et al.'', Maurotoxin, a four disulfide bridges scorpion toxin acting on K+ channels. Toxicon, 1998. 36(11): p. 1609-111609–11.
# Visan, V., ''et al.'', Mapping of maurotoxin binding sites on hKv1.2, hKv1.3, and hIKCa1 channels. Mol Pharmacol, 2004. 66(5): p. 1103-121103–12.
 
{{Toxins}}
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[[Category:Neurotoxins]]
[[Category:Ion channel toxins]]
[[Category:InvertebrateScorpion toxins]]