| Structural highlights
8dn3 is a 5 chain structure with sequence from Aequorea victoria and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | Electron Microscopy, Resolution 3.55Å |
| Ligands: | , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Disease
GLRB_HUMAN Hereditary hyperekplexia. The disease is caused by variants affecting the gene represented in this entry.
Function
GLRB_HUMAN Glycine receptors are ligand-gated chloride channels. GLRB does not form ligand-gated ion channels by itself, but is part of heteromeric ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:8717357, PubMed:15302677, PubMed:16144831, PubMed:22715885, PubMed:25445488, PubMed:11929858, PubMed:23238346). Heteropentameric channels composed of GLRB and GLRA1 are activated by lower glycine levels than homopentameric GLRA1 (PubMed:8717357). Plays an important role in the down-regulation of neuronal excitability (PubMed:11929858, PubMed:23238346). Contributes to the generation of inhibitory postsynaptic currents (PubMed:25445488).[1] [2] [3] [4] [5] [6] [7] GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
References
- ↑ Rees MI, Lewis TM, Kwok JB, Mortier GR, Govaert P, Snell RG, Schofield PR, Owen MJ. Hyperekplexia associated with compound heterozygote mutations in the beta-subunit of the human inhibitory glycine receptor (GLRB). Hum Mol Genet. 2002 Apr 1;11(7):853-60. PMID:11929858 doi:10.1093/hmg/11.7.853
- ↑ 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
- ↑ 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
- ↑ Yang Z, Taran E, Webb TI, Lynch JW. Stoichiometry and subunit arrangement of α1β glycine receptors as determined by atomic force microscopy. Biochemistry. 2012 Jul 3;51(26):5229-31. PMID:22715885 doi:10.1021/bi300063m
- ↑ James VM, Bode A, Chung SK, Gill JL, Nielsen M, Cowan FM, Vujic M, Thomas RH, Rees MI, Harvey K, Keramidas A, Topf M, Ginjaar I, Lynch JW, Harvey RJ. Novel missense mutations in the glycine receptor β subunit gene (GLRB) in startle disease. Neurobiol Dis. 2013 Apr;52:137-49. PMID:23238346 doi:10.1016/j.nbd.2012.12.001
- ↑ 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
- ↑ Handford CA, Lynch JW, Baker E, Webb GC, Ford JH, Sutherland GR, Schofield PR. The human glycine receptor beta subunit: primary structure, functional characterisation and chromosomal localisation of the human and murine genes. Brain Res Mol Brain Res. 1996 Jan;35(1-2):211-9 PMID:8717357
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