6N51
Metabotropic Glutamate Receptor 5 bound to L-quisqualate and Nb43
Summary for 6N51
Entry DOI | 10.2210/pdb6n51/pdb |
Related | 6N4X 6N4Y 6N50 6N51 6N52 |
EMDB information | 0345 0346 0347 |
Descriptor | Metabotropic glutamate receptor 5, Nanobody 43, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | cell surface receptor, membrane protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 4 |
Total formula weight | 208942.04 |
Authors | Koehl, A.,Hu, H.,Feng, D.,Sun, B.,Weis, W.I.,Skiniotis, G.S.,Mathiesen, J.M.,Kobilka, B.K. (deposition date: 2018-11-20, release date: 2019-01-23, Last modification date: 2020-07-29) |
Primary citation | Koehl, A.,Hu, H.,Feng, D.,Sun, B.,Zhang, Y.,Robertson, M.J.,Chu, M.,Kobilka, T.S.,Laermans, T.,Steyaert, J.,Tarrasch, J.,Dutta, S.,Fonseca, R.,Weis, W.I.,Mathiesen, J.M.,Skiniotis, G.,Kobilka, B.K. Structural insights into the activation of metabotropic glutamate receptors. Nature, 566:79-84, 2019 Cited by PubMed Abstract: Metabotropic glutamate receptors are family C G-protein-coupled receptors. They form obligate dimers and possess extracellular ligand-binding Venus flytrap domains, which are linked by cysteine-rich domains to their 7-transmembrane domains. Spectroscopic studies show that signalling is a dynamic process, in which large-scale conformational changes underlie the transmission of signals from the extracellular Venus flytraps to the G protein-coupling domains-the 7-transmembrane domains-in the membrane. Here, using a combination of X-ray crystallography, cryo-electron microscopy and signalling studies, we present a structural framework for the activation mechanism of metabotropic glutamate receptor subtype 5. Our results show that agonist binding at the Venus flytraps leads to a compaction of the intersubunit dimer interface, thereby bringing the cysteine-rich domains into close proximity. Interactions between the cysteine-rich domains and the second extracellular loops of the receptor enable the rigid-body repositioning of the 7-transmembrane domains, which come into contact with each other to initiate signalling. PubMed: 30675062DOI: 10.1038/s41586-019-0881-4 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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