1, The glycine receptor channel (GlyR), a member of the ligand-gated ion ch
annel superfamily; shares many similar permeation properties with the GABAA
receptor channel.
2, The GlyR is anion permeable, with P-K/P-Cl < 0,05, has a 5-6 Angstrom mi
nimum pore diameter and a permeation selectivity sequence dominated by hydr
ation energies.
3, The channels, which display multiple subconductance states, can be multi
ply occupied,
4 Two positive arginine rings at the ends of the pore region may contribute
to the anion selectivity of the GlyR,
5, Mutation of the extracellular charged arginine ring can impair channel f
unction by decreasing the sensitivity of glycine activation, reducing chann
el conductance, shifting the normal multi-subconductance states to lower va
lues and by decoupling the link between ligand binding and channel gating,
6, These and other site-directed mutagenesis studies of recombinant GlyR;RI
together with studies of native GlyR, are providing further insights into
what controls gating and ion permeation and selectivity through this channe
l.