Abstract
The molecular determinants of the ionic selectivity and single-channel conductance of the Cys-loop family of transmitter-gated ion channels are beginning to be understood with increasing precision, in part, as a result of the recent availability of refined ultrastructural information for the archetype of the family, the nicotinic acetylcholine receptor (nAChR). Studies of another member of this family, the 5-HT(3) receptor, have now provided insight into the structure of its channel pore, the location of its gate and mechanisms of ion selectivity and translocation. The anomaly of the extremely low single-channel conductance of the homo-oligomeric 5-HT(3A) receptor has recently been solved, revealing that an intracellular domain of the protein is an important determinant of single-channel conductance. Such data are interpreted, in this article, in light of the most recent developments in structural characterization of the nAChR.
| Original language | English |
|---|---|
| Pages (from-to) | 587-94 |
| Number of pages | 8 |
| Journal | Trends in Pharmacological Sciences |
| Volume | 26 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - Nov 2005 |
Keywords
- Amino Acid Sequence
- Animals
- Cysteine/chemistry
- Humans
- Ion Channel Gating
- Ion Channels/chemistry
- Ions
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Protein Structure, Quaternary
- Protein Structure, Tertiary
- Receptors, Nicotinic/chemistry
- Receptors, Serotonin, 5-HT3/chemistry