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	Structural insight into apelin receptor-G protein stoichiometry.
Journal, issue, pages	Nat Struct Mol Biol, Vol. 29, Issue 7, Page 688-697, Year 2022
Publish date	Jul 11, 2022
Authors	Yang Yue / Lier Liu / Li-Jie Wu / Yiran Wu / Ling Wang / Fei Li / Junlin Liu / Gye-Won Han / Bo Chen / Xi Lin / Rebecca L Brouillette / Émile Breault / Jean-Michel Longpré / Songting Shi / Hui Lei / Philippe Sarret / Raymond C Stevens / Michael A Hanson / Fei Xu /
PubMed Abstract	The technique of cryogenic-electron microscopy (cryo-EM) has revolutionized the field of membrane protein structure and function with a focus on the dominantly observed molecular species. This report ...The technique of cryogenic-electron microscopy (cryo-EM) has revolutionized the field of membrane protein structure and function with a focus on the dominantly observed molecular species. This report describes the structural characterization of a fully active human apelin receptor (APJR) complexed with heterotrimeric G protein observed in both 2:1 and 1:1 stoichiometric ratios. We use cryo-EM single-particle analysis to determine the structural details of both species from the same sample preparation. Protein preparations, in the presence of the endogenous peptide ligand ELA or a synthetic small molecule, both demonstrate these mixed stoichiometric states. Structural differences in G protein engagement between dimeric and monomeric APJR suggest a role for the stoichiometry of G protein-coupled receptor- (GPCR-)G protein coupling on downstream signaling and receptor pharmacology. Furthermore, a small, hydrophobic dimer interface provides a starting framework for additional class A GPCR dimerization studies. Together, these findings uncover a mechanism of versatile regulation through oligomerization by which GPCRs can modulate their signaling.
External links	Nat Struct Mol Biol / PubMed:35817871
Methods	EM (single particle) / X-ray diffraction
Resolution	2.7 - 4.21 Å
Structure data	32243 7w0l EMDB-32243, PDB-7w0l: Cryo-EM structure of a dimeric GPCR-Gi complex with small molecule Method: EM (single particle) / Resolution: 3.57 Å 32244 7w0m EMDB-32244, PDB-7w0m: Cryo-EM structure of a monomeric GPCR-Gi complex with small molecule Method: EM (single particle) / Resolution: 3.71 Å 32245 7w0n EMDB-32245, PDB-7w0n: Cryo-EM structure of a dimeric GPCR-Gi complex with peptide Method: EM (single particle) / Resolution: 4.21 Å 32246 7w0o EMDB-32246, PDB-7w0o: Cryo-EM structure of a monomeric GPCR-Gi complex with peptide Method: EM (single particle) / Resolution: 3.78 Å 32247 7w0p EMDB-32247, PDB-7w0p: Cryo-EM structure of a GPCR-Gi complex with peptide Method: EM (single particle) / Resolution: 3.16 Å PDB-7sus: Crystal structure of Apelin receptor in complex with small molecule Method: X-RAY DIFFRACTION / Resolution: 2.7 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-8EH: (1R,2S)-N-[4-(2,6-dimethoxyphenyl)-5-(6-methylpyridin-2-yl)-1,2,4-triazol-3-yl]-1-(5-methylpyrimidin-2-yl)-1-oxidanyl-propane-2-sulfonamide ChemComp-OLC: (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate ChemComp-HOH: WATER / Water
Source	homo sapiens (human) clostridium pasteurianum (bacteria) escherichia coli (E. coli)
Keywords	MEMBRANE PROTEIN / GPCR / Class A GPCR / small molecule / Apelin receptor / Complex / Dimerization