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Charge selectivity of the Cys‐loop family of ligand‐gated ion channels
Author(s) -
Jensen Marianne L.,
Schousboe Arne,
Ahring Philip K.
Publication year - 2005
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2004.02883.x
Subject(s) - homomeric , ligand gated ion channel , selectivity , chemistry , ion channel , glycine receptor , receptor , transmembrane domain , biophysics , light gated ion channel , ligand (biochemistry) , nicotinic acetylcholine receptor , acetylcholine receptor , amino acid , protein subunit , glycine , biochemistry , biology , gene , catalysis
The determinants of charge selectivity of the Cys‐loop family of ligand‐gated ion channels have been studied for more than a decade. The investigations have mainly covered homomeric receptors e.g. the nicotinic acetylcholine receptor α 7 , the glycine receptor α 1 and the serotonin receptor 5‐HT 3A . Only recently, the determinants of charge selectivity of heteromeric receptors have been addressed for the GABA A receptor α 2 β 3 γ 2 . For all receptor subtypes, the selectivity determinants have been located to an intracellular linker between transmembrane domains M1 and M2. Two features of the M1–M2 linker appear to control ion selectivity. A central role for charged amino acid residues in selectivity has been almost universally observed. Furthermore, recent studies point to an important role of the size of the narrowest constriction in the pore. In the present review, these determinants of charge selectivity of the Cys‐loop family of ligand‐gated ion channels will be discussed in detail.