The contribution of proline 250 (P-2') to pore diameter and ion selectivity in the human glycine receptor channel
The glycine receptor-channel (GlyR) mediates neuronal inhibition by selectively allowing the passage of Cl(-) ions through its channel. The pore region for ion selectivity is localised to the constricted internal end of the M2 transmembrane domain. This paper investigates the contribution of the P-2' residue in determining pore diameter and ion charge selectivity of the GlyR. The deletion of this proline has been shown to decrease the anion/cation permeability ratio, with P(Cl)/P(Na) decreasing from approximately 27 to approximately 4. We show that the P-2' deletion by itself produces a GlyR with a larger pore diameter ( approximately 0.69 nm) than the wild type value ( approximately 0.54 nm). This confirms that the P-2' residue reduces pore size, which suggests that, in addition to electrostatic effects, pore size also contributes to ion-charge selectivity.
|Authors||Lee, D. J.;Keramidas, A.;Moorhouse, A. J.;Schofield, P. R.;Barry, P. H. :|
|Publisher Name||NEUROSCIENCE LETTERS|
|Published Date||2003-01-01 00:00:00|
|URL link to publisher's version||http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14623139|
|OpenAccess link to author's accepted manuscript version||https://publications.gimr.garvan.org.au/open-access/1692|