8T8M
Quis-bound intermediate mGlu5
Summary for 8T8M
| Entry DOI | 10.2210/pdb8t8m/pdb |
| EMDB information | 41099 41803 41804 |
| Descriptor | Metabotropic glutamate receptor 5, Nb43, (S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID (3 entities in total) |
| Functional Keywords | gpcr, signaling protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 224824.19 |
| Authors | Krishna Kumar, K.,Wang, H.,Kobilka, B.K. (deposition date: 2023-06-22, release date: 2023-10-11, Last modification date: 2025-05-21) |
| Primary citation | Krishna Kumar, K.,Wang, H.,Habrian, C.,Latorraca, N.R.,Xu, J.,O'Brien, E.S.,Zhang, C.,Montabana, E.,Koehl, A.,Marqusee, S.,Isacoff, E.Y.,Kobilka, B.K. Stepwise activation of a metabotropic glutamate receptor. Nature, 629:951-956, 2024 Cited by PubMed Abstract: Metabotropic glutamate receptors belong to a family of G protein-coupled receptors that are obligate dimers and possess a large extracellular ligand-binding domain that is linked via a cysteine-rich domain to their 7-transmembrane domain. Upon activation, these receptors undergo a large conformational change to transmit the ligand binding signal from the extracellular ligand-binding domain to the G protein-coupling 7-transmembrane domain. In this manuscript, we propose a model for a sequential, multistep activation mechanism of metabotropic glutamate receptor subtype 5. We present a series of structures in lipid nanodiscs, from inactive to fully active, including agonist-bound intermediate states. Further, using bulk and single-molecule fluorescence imaging, we reveal distinct receptor conformations upon allosteric modulator and G protein binding. PubMed: 38632403DOI: 10.1038/s41586-024-07327-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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