Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic
- 1 October 1992
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 359 (6395) , 500-505
- https://doi.org/10.1038/359500a0
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.Keywords
This publication has 46 references indexed in Scilit:
- In the GluR1 glutamate receptor subunit a glutamine to histidine point mutation suppresses inward rectification but not calcium permeabilityBiochemical and Biophysical Research Communications, 1992
- A ring of uncharged polar amino acids as a component of channel constriction in the nicotinic acetylcholine receptorFEBS Letters, 1991
- Role of a key cysteine residue in the gating of the acetylcholine receptorNeuron, 1991
- A neuronal nicotinic acetylcholine receptor subunit (α7) is developmentally regulated and forms a homo-oligomeric channel blocked by α-BTXNeuron, 1990
- Chloride channels of biological membranesBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1990
- The structure of ion channels in membranes of excitable cellsNeuron, 1989
- Structure of the high-affinity binding site for noncompetitive blockers of the acetylcholine receptor: [3H]chlorpromazine labels homologous residues in the .beta. and .delta. chainsBiochemistry, 1987
- The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices M II of the receptor subunitsFEBS Letters, 1986
- Conformations of Torpedo acetylcholine receptor associated with ion transport and desensitizationBiochemistry, 1982
- Single acetylcholine-activated channels show burst-kinetics in presence of desensitizing concentrations of agonistNature, 1980