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The nicotinic acetylcholine receptor (nAChR) is a cation-selective ion channel that opens in response to acetylcholine binding. The related glycine receptor (GlyR) is anion selective. The pore-lining domain of each protein may be modeled as a bundle of five parallel M2 helices. Models of the pore-lining domains of homopentameric nAChR and GlyR have been used in continuum electrostatics calculations to probe the origins of ion selectivity. Calculated pKA values suggest that "rings" of acidic or basic side chains at the mouths of the nAChR or GlyR M2 helix bundles, respectively, may not be fully ionized. In particular, for the nAChR the ring of glutamate side chains at the extracellular mouth of the pore is predicted to be largely protonated at neutral pH, whereas those glutamate side chains in the intracellular and intermediate rings (at the opposite mouth of the pore) are predicted to be fully ionized. Inclusion of the other domains of each protein represented as an irregular cylindrical tube in which the M2 bundles are embedded suggests that both the M2 helices and the extramembrane domains play significant roles in determining ion selectivity.

Original publication




Journal article


Biophys J

Publication Date





1211 - 1222


Amino Acid Sequence, Animals, Biophysical Phenomena, Biophysics, Chickens, Humans, Ion Channel Gating, Ion Channels, Ligands, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Receptors, Glycine, Receptors, Nicotinic, Static Electricity, Thermodynamics