| Title : Molecular basis of the charge selectivity of nicotinic acetylcholine receptor and related ligand-gated ion channels - Corringer_1999_Novartis.Found.Symp_225_215 |
| Author(s) : Corringer PJ , Bertrand S , Galzi JL , Devillers-Thiery A , Changeux JP , Bertrand D |
| Ref : Novartis Found Symp , 225 :215 , 1999 |
| Abstract : Nicotinic acetylcholine receptors are homo- or heteropentameric proteins belonging to the superfamily of receptor channels including the glycine and GABA-A receptors. Affinity labelling and mutagenesis experiments indicated that the M2 transmembrane segment of each subunit lines the ion channel and is coiled into an alpha-helix. Comparison of the M2 sequence of the cation-selective alpha 7 nicotinic receptor to that of the anion-selective alpha 1 glycine receptor identified amino acids involved in charge selectivity. Mutations of the alpha 7 homo-oligomeric receptor within (or near) M2, namely E237A, V251T and a proline insertion P236' were shown to convert the ionic selectivity of alpha 7 from cationic to anionic. Systematic analysis of each of these three mutations supports the notion that the conversion of ionic selectivity results from a local structural reorganization of the 234-238 loop. The 234-238 coiled loop, previously shown to lie near the narrowest portion of the channel, is thus proposed to contribute directly to the charge selectivity filter. A possible functional analogy with the voltage-gated ion channels and related receptors is discussed. |
| ESTHER : Corringer_1999_Novartis.Found.Symp_225_215 |
| PubMedSearch : Corringer_1999_Novartis.Found.Symp_225_215 |
| PubMedID: 10472058 |
Corringer PJ, Bertrand S, Galzi JL, Devillers-Thiery A, Changeux JP, Bertrand D (1999)
Molecular basis of the charge selectivity of nicotinic acetylcholine receptor and related ligand-gated ion channels
Novartis Found Symp
225 :215
Corringer PJ, Bertrand S, Galzi JL, Devillers-Thiery A, Changeux JP, Bertrand D (1999)
Novartis Found Symp
225 :215