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6N51

Metabotropic Glutamate Receptor 5 bound to L-quisqualate and Nb43

Summary for 6N51
Entry DOI10.2210/pdb6n51/pdb
Related6N4X 6N4Y 6N50 6N51 6N52
EMDB information0345 0346 0347
DescriptorMetabotropic glutamate receptor 5, Nanobody 43, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordscell surface receptor, membrane protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight208942.04
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 citationKoehl, 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: 30675062
DOI: 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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