Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structures of human mGlu2 and mGlu7 homo- and heterodimers.
Journal, issue, pages	Nature, Vol. 594, Issue 7864, Page 589-593, Year 2021
Publish date	Jun 16, 2021
Authors	Juan Du / Dejian Wang / Hongcheng Fan / Chanjuan Xu / Linhua Tai / Shuling Lin / Shuo Han / Qiuxiang Tan / Xinwei Wang / Tuo Xu / Hui Zhang / Xiaojing Chu / Cuiying Yi / Peng Liu / Xiaomei Wang / Yu Zhou / Jean-Philippe Pin / Philippe Rondard / Hong Liu / Jianfeng Liu / Fei Sun / Beili Wu / Qiang Zhao /
PubMed Abstract	The metabotropic glutamate receptors (mGlus) are involved in the modulation of synaptic transmission and neuronal excitability in the central nervous system. These receptors probably exist as both ...The metabotropic glutamate receptors (mGlus) are involved in the modulation of synaptic transmission and neuronal excitability in the central nervous system. These receptors probably exist as both homo- and heterodimers that have unique pharmacological and functional properties. Here we report four cryo-electron microscopy structures of the human mGlu subtypes mGlu2 and mGlu7, including inactive mGlu2 and mGlu7 homodimers; mGlu2 homodimer bound to an agonist and a positive allosteric modulator; and inactive mGlu2-mGlu7 heterodimer. We observed a subtype-dependent dimerization mode for these mGlus, as a unique dimer interface that is mediated by helix IV (and that is important for limiting receptor activity) exists only in the inactive mGlu2 structure. The structures provide molecular details of the inter- and intra-subunit conformational changes that are required for receptor activation, which distinguish class C G-protein-coupled receptors from those in classes A and B. Furthermore, our structure and functional studies of the mGlu2-mGlu7 heterodimer suggest that the mGlu7 subunit has a dominant role in controlling dimeric association and G-protein activation in the heterodimer. These insights into mGlu homo- and heterodimers highlight the complex landscape of mGlu dimerization and activation.
External links	Nature / PubMed:34135509
Methods	EM (single particle) / X-ray diffraction
Resolution	2.5 - 4.0 Å
Structure data	31235 7epa EMDB-31235, PDB-7epa: Cryo-EM structure of inactive mGlu2 homodimer Method: EM (single particle) / Resolution: 3.6 Å 31236 7epb EMDB-31236, PDB-7epb: Cryo-EM structure of LY354740-bound mGlu2 homodimer Method: EM (single particle) / Resolution: 3.1 Å 31237 7epc EMDB-31237, PDB-7epc: Cryo-EM structure of inactive mGlu7 homodimer Method: EM (single particle) / Resolution: 4.0 Å 31238 7epd EMDB-31238, PDB-7epd: Cryo-EM structure of inactive mGlu2-7 heterodimer Method: EM (single particle) / Resolution: 3.9 Å PDB-7epe: Crystal structure of mGlu2 bound to NAM563 Method: X-RAY DIFFRACTION / Resolution: 2.5 Å PDB-7epf: Crystal structure of mGlu2 bound to NAM597 Method: X-RAY DIFFRACTION / Resolution: 2.7 Å
Chemicals	ChemComp-40F: (1S,2S,5R,6S)-2-aminobicyclo[3.1.0]hexane-2,6-dicarboxylic acid / Eglumetad ChemComp-FMN: FLAVIN MONONUCLEOTIDE / Flavin mononucleotide ChemComp-J9R: 4-(1-methylpyrazol-4-yl)-7-[[(2~{S})-2-(trifluoromethyl)morpholin-4-yl]methyl]quinoline-2-carboxamide ChemComp-J9U: (8~{R})-4-[2,4-bis(fluoranyl)phenyl]-8-methyl-7-[(2-methylpyrazol-3-yl)methyl]-6,8-dihydro-5~{H}-1,7-naphthyridine-2-carboxamide
Source	homo sapiens (human) lama glama (llama)
Keywords	MEMBRANE PROTEIN / cryo-EM structure / GPCR