7MLV
Cryo-EM reveals partially and fully assembled native glycine receptors,homomeric tetramer
Summary for 7MLV
| Entry DOI | 10.2210/pdb7mlv/pdb |
| EMDB information | 23911 |
| Descriptor | 3D1 Fab Light Chain, 3D1 Fab Heavy Chain, Glycine receptor alpha 1, ... (9 entities in total) |
| Functional Keywords | glycine receptor, ion channel, homomeric tetramer, membrane protein, signaling protein |
| Biological source | Rattus norvegicus More |
| Total number of polymer chains | 12 |
| Total formula weight | 313561.21 |
| Authors | Zhu, H.,Gouaux, E. (deposition date: 2021-04-29, release date: 2021-09-29, Last modification date: 2024-10-09) |
| Primary citation | Zhu, H.,Gouaux, E. Architecture and assembly mechanism of native glycine receptors. Nature, 599:513-517, 2021 Cited by PubMed Abstract: Glycine receptors (GlyRs) are pentameric, 'Cys-loop' receptors that form chloride-permeable channels and mediate fast inhibitory signalling throughout the central nervous system. In the spinal cord and brainstem, GlyRs regulate locomotion and cause movement disorders when mutated. However, the stoichiometry of native GlyRs and the mechanism by which they are assembled remain unclear, despite extensive investigation. Here we report cryo-electron microscopy structures of native GlyRs from pig spinal cord and brainstem, revealing structural insights into heteromeric receptors and their predominant subunit stoichiometry of 4α:1β. Within the heteromeric pentamer, the β(+)-α(-) interface adopts a structure that is distinct from the α(+)-α(-) and α(+)-β(-) interfaces. Furthermore, the β-subunit contains a unique phenylalanine residue that resides within the pore and disrupts the canonical picrotoxin site. These results explain why inclusion of the β-subunit breaks receptor symmetry and alters ion channel pharmacology. We also find incomplete receptor complexes and, by elucidating their structures, reveal the architectures of partially assembled α-trimers and α-tetramers. PubMed: 34555840DOI: 10.1038/s41586-021-04022-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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