Title : Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic - Galzi_1992_Nature_359_500 |
Author(s) : Galzi JL , Devillers-Thiery A , Hussy N , Bertrand S , Changeux JP , Bertrand D |
Ref : Nature , 359 :500 , 1992 |
Abstract :
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. |
PubMedSearch : Galzi_1992_Nature_359_500 |
PubMedID: 1383829 |
Galzi JL, Devillers-Thiery A, Hussy N, Bertrand S, Changeux JP, Bertrand D (1992)
Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic
Nature
359 :500
Galzi JL, Devillers-Thiery A, Hussy N, Bertrand S, Changeux JP, Bertrand D (1992)
Nature
359 :500