6pm2 | pdb_00006pm2

CryoEM structure of zebra fish alpha-1 glycine receptor bound with Taurine in SMA, open state

spinqualitylabelsall models 6pm2, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6pm2 is a 5 chain structure with sequence from Brachidanio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, TAU, NAG Gene: glra1 (Brachidanio rerio) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GLRA1_DANRE] Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:10188956, PubMed:26344198). Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents. Channel activity is potentiated by ethanol (By similarity).[UniProtKB:P23415] Publication Abstract from PubMed Ligand-gated ion channels mediate signal transduction at chemical synapses and transition between resting, open, and desensitized states in response to neurotransmitter binding. Neurotransmitters that produce maximum open channel probabilities (Po) are full agonists, whereas those that yield lower than maximum Po are partial agonists. Cys-loop receptors are an important class of neurotransmitter receptors, yet a structure-based understanding of the mechanism of partial agonist action has proven elusive. Here, we study the glycine receptor with the full agonist glycine and the partial agonists taurine and gamma-amino butyric acid (GABA). We use electrophysiology to show how partial agonists populate agonist-bound, closed channel states and cryo-EM reconstructions to illuminate the structures of intermediate, pre-open states, providing insights into previously unseen conformational states along the receptor reaction pathway. We further correlate agonist-induced conformational changes to Po across members of the receptor family, providing a hypothetical mechanism for partial and full agonist action at Cys-loop receptors. Mechanism of gating and partial agonist action in the glycine receptor.,Yu J, Zhu H, Lape R, Greiner T, Du J, Lu W, Sivilotti L, Gouaux E Cell. 2021 Feb 18;184(4):957-968.e21. doi: 10.1016/j.cell.2021.01.026. Epub 2021 , Feb 9. PMID:33567265 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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