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• W2021750986 abstract "The α/β scorpion fold is shared by scorpion toxins, insect defensins, and plant thionins. This small and functionally versatile template contains an α-helix and a triple β-sheet linked by three disulfide bridges. With the view to introduce novel functional centers within this fold, we replaced the sequence (the cysteines and glycines excepted) of the original β-hairpin of a scorpion toxin by the sequence of a β-hairpin that forms part of the site by which snake neurotoxins bind to nicotinic acetylcholine receptors (AcChOR). The resulting chimeric protein, synthesized by chemical means, binds to AcChOR, though with a lower affinity than the snake toxins [Drakopoulou, E., Zinn-Justin, S., Guenneugues, M., Gilquin, B., Ménez, A., & Vita, C. (1996) J. Biol. Chem. 271, 11979−11987]. The work described in this paper is an attempt to clarify the structural consequences associated with the transfer of the β-hairpin. We report the determination of the three-dimensional solution structure of the chimeric protein by proton NMR spectroscopy and molecular dynamics calculations. Comparison of the structure of the chimera with those of the scorpion α/β toxin and of the snake neurotoxin shows that (i) the new protein folds as an α/β motif and (ii) the β-hairpins of the chimera and of the curaremimetic toxin adopt a similar conformation. A closer inspection of the differences between the structures of the original and transferred β-hairpins allows rationalization of the biological properties of the chimera." @default.
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• W2021750986 date "1996-01-01" @default.
• W2021750986 modified "2023-10-18" @default.
• W2021750986 title "Transfer of a β-Hairpin from the Functional Site of Snake Curaremimetic Toxins to the α/β Scaffold of Scorpion Toxins: Three-Dimensional Solution Structure of the Chimeric Protein^," @default.
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• W2021750986 doi "https://doi.org/10.1021/bi960466n" @default.
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