6PM2
CryoEM structure of zebra fish alpha-1 glycine receptor bound with Taurine in SMA, open state
Summary for 6PM2
| Entry DOI | 10.2210/pdb6pm2/pdb |
| EMDB information | 20384 |
| Descriptor | Glycine receptor subunit alphaZ1, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-AMINOETHANESULFONIC ACID (3 entities in total) |
| Functional Keywords | glycine receptor, sma, cryoem, membrane protein |
| Biological source | Danio rerio (Zebrafish) |
| Total number of polymer chains | 5 |
| Total formula weight | 266246.43 |
| Authors | Yu, J.,Zhu, H.,Gouaux, E. (deposition date: 2019-07-01, release date: 2021-02-10, Last modification date: 2024-10-23) |
| Primary citation | Yu, J.,Zhu, H.,Lape, R.,Greiner, T.,Du, J.,Lu, W.,Sivilotti, L.,Gouaux, E. Mechanism of gating and partial agonist action in the glycine receptor. Cell, 184:957-968.e21, 2021 Cited by PubMed Abstract: 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 γ-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. PubMed: 33567265DOI: 10.1016/j.cell.2021.01.026 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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