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XB-ART-23292
Nature 1992 Oct 08;3596395:500-5. doi: 10.1038/359500a0.
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Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic.

Galzi JL , Devillers-Thiéry A , Hussy N , Bertrand S , Changeux JP , Bertrand D .


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Introduction by site-directed mutagenesis of three amino acids from the MII segment of glycine or gamma-aminobutyric acid (GABAA) receptors into the MII segment of alpha 7 nicotinic receptor was sufficient to convert a cation-selective channel into an anion-selective channel gated by acetylcholine. A critical mutation was the insertion of an uncharged residue at the amino-terminal end of MII, stressing the importance of protein geometrical constraints on ion selectivity.

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Species referenced: Xenopus
Genes referenced: gabarap