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Cyro-EM structure of human Glycine Receptor alpha2-beta heteromer, strychnine bound state, 3.8 AngstromCyro-EM structure of human Glycine Receptor alpha2-beta heteromer, strychnine bound state, 3.8 Angstrom
Structural highlights
DiseaseGLRA2_HUMAN The disease is caused by variants affecting the gene represented in this entry. FunctionGLRA2_HUMAN Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:15302677, PubMed:16144831, PubMed:2155780, PubMed:23895467, PubMed:25445488, PubMed:26370147, PubMed:34473954). 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] [6] See AlsoReferences
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