Abstract
Introduction by site-directed mutagenesis of three amino acids from the Mil segment of glycine or & GAMMA;-aminobutyric acid (GABAA) receptors into the Mil segment of α7 nicotinic receptor was sufficient to convert a cation-selective channel into an an ion-selective channel gated by acetylcholine. A critical mutation was the insertion of an uncharged residue at the amino-terminal end of Mil, stressing the importance of protein geometrical constraints on ion selectivity.
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secCl is a cys-loop ion channel necessary for the chloride conductance that mediates hormone-induced fluid secretion in Drosophila
Scientific Reports Open Access 16 May 2019
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Galzi, JL., Devillers-Thiery, A., Hussy, N. et al. Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic. Nature 359, 500–505 (1992). https://doi.org/10.1038/359500a0
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DOI: https://doi.org/10.1038/359500a0
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