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XB-ART-10381
J Biol Chem 2000 Dec 15;27550:39394-402. doi: 10.1074/jbc.M006810200.
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Maurotoxin versus Pi1/HsTx1 scorpion toxins. Toward new insights in the understanding of their distinct disulfide bridge patterns.

Fajloun Z, Mosbah A, Carlier E, Mansuelle P, Sandoz G, Fathallah M, di Luccio E, Devaux C, Rochat H, Darbon H, De Waard M, Sabatier JM.


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Maurotoxin (MTX) is a scorpion toxin acting on several K(+) channel subtypes. It is a 34-residue peptide cross-linked by four disulfide bridges that are in an "uncommon" arrangement of the type C1-C5, C2-C6, C3-C4, and C7-C8 (versus C1-C5, C2-C6, C3-C7, and C4-C8 for Pi1 or HsTx1, two MTX-related scorpion toxins). We report here that a single mutation in MTX, in either position 15 or 33, resulted in a shift from the MTX toward the Pi1/HsTx1 disulfide bridge pattern. This shift is accompanied by structural and pharmacological changes of the peptide without altering the general alpha/beta scaffold of scorpion toxins.

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???displayArticle.link??? J Biol Chem