5bkf

Structural highlights

Disease

GLRA2_HUMAN The disease is caused by variants affecting the gene represented in this entry.

Function

GLRA2_HUMAN Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:2155780, PubMed:15302677, PubMed:16144831, PubMed:23895467, PubMed:25445488, PubMed:26370147). Channel opening is also triggered by taurine and beta-alanine (PubMed:15302677). Plays a role in synaptic plasticity (By similarity). Contributes to the generation of inhibitory postsynaptic currents, and is involved in the down-regulation of neuronal excitability (PubMed:25445488). Plays a role in cellular responses to ethanol (PubMed:23895467).[UniProtKB:Q7TNC8]^{[1] [2] [3] [4] [5]}

See Also

• Green Fluorescent Protein 3D structures

References

1. ↑ Miller PS, Harvey RJ, Smart TG. Differential agonist sensitivity of glycine receptor alpha2 subunit splice variants. Br J Pharmacol. 2004 Sep;143(1):19-26. PMID:15302677 doi:10.1038/sj.bjp.0705875
2. ↑ Miller PS, Da Silva HM, Smart TG. Molecular basis for zinc potentiation at strychnine-sensitive glycine receptors. J Biol Chem. 2005 Nov 11;280(45):37877-84. PMID:16144831 doi:10.1074/jbc.M508303200
3. ↑ Grenningloh G, Schmieden V, Schofield PR, Seeburg PH, Siddique T, Mohandas TK, Becker CM, Betz H. Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes. EMBO J. 1990 Mar;9(3):771-6. PMID:2155780 doi:10.1002/j.1460-2075.1990.tb08172.x
4. ↑ McCracken LM, Trudell JR, McCracken ML, Harris RA. Zinc-dependent modulation of α2 Alcohol Clin Exp Res. 2013 Dec;37(12):2002-10. PMID:23895467 doi:10.1111/acer.12192
5. ↑ Zhang Y, Dixon CL, Keramidas A, Lynch JW. Functional reconstitution of glycinergic synapses incorporating defined glycine receptor subunit combinations. Neuropharmacology. 2015 Feb;89:391-7. PMID:25445488 doi:10.1016/j.neuropharm.2014.10.026