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 atypical chemokine receptor 3 reveal the basis for its promiscuity and signaling bias.
Journal, issue, pages	Sci Adv, Vol. 8, Issue 28, Page eabn8063, Year 2022
Publish date	Jul 15, 2022
Authors	Yu-Chen Yen / Christopher T Schafer / Martin Gustavsson / Stefanie A Eberle / Pawel K Dominik / Dawid Deneka / Penglie Zhang / Thomas J Schall / Anthony A Kossiakoff / John J G Tesmer / Tracy M Handel /
PubMed Abstract	Both CXC chemokine receptor 4 (CXCR4) and atypical chemokine receptor 3 (ACKR3) are activated by the chemokine CXCL12 yet evoke distinct cellular responses. CXCR4 is a canonical G protein-coupled ...Both CXC chemokine receptor 4 (CXCR4) and atypical chemokine receptor 3 (ACKR3) are activated by the chemokine CXCL12 yet evoke distinct cellular responses. CXCR4 is a canonical G protein-coupled receptor (GPCR), whereas ACKR3 is intrinsically biased for arrestin. The molecular basis for this difference is not understood. Here, we describe cryo-EM structures of ACKR3 in complex with CXCL12, a more potent CXCL12 variant, and a small-molecule agonist. The bound chemokines adopt an unexpected pose relative to those established for CXCR4 and observed in other receptor-chemokine complexes. Along with functional studies, these structures provide insight into the ligand-binding promiscuity of ACKR3, why it fails to couple to G proteins, and its bias toward β-arrestin. The results lay the groundwork for understanding the physiological interplay of ACKR3 with other GPCRs.
External links	Sci Adv / PubMed:35857509 / PubMed Central
Methods	EM (single particle)
Resolution	3.3 - 4.0 Å
Structure data	25171 7sk3 EMDB-25171, PDB-7sk3: Cryo-EM structure of ACKR3 in complex with CXCL12, an intracellular Fab, and an extracellular Fab Method: EM (single particle) / Resolution: 3.8 Å 25172 7sk4 EMDB-25172, PDB-7sk4: Cryo-EM structure of ACKR3 in complex with chemokine N-terminal mutant CXCL12_LRHQ, an intracellular Fab, and an extracellular Fab Method: EM (single particle) / Resolution: 3.3 Å 25173 7sk5 EMDB-25173, PDB-7sk5: Cryo-EM structure of ACKR3 in complex with CXCL12 and an intracellular Fab Method: EM (single particle) / Resolution: 4.0 Å 25174 7sk6 EMDB-25174, PDB-7sk6: Cryo-EM structure of human ACKR3 in complex with chemokine N-terminal mutant CXCL12_LRHQ and an intracellular Fab Method: EM (single particle) / Resolution: 4.0 Å 25175 7sk7 EMDB-25175, PDB-7sk7: Cryo-EM structure of human ACKR3 in complex with CXCL12, a small molecule partial agonist CCX662, and an extracellular Fab Method: EM (single particle) / Resolution: 3.3 Å 25176 7sk8 EMDB-25176, PDB-7sk8: Cryo-EM structure of human ACKR3 in complex with CXCL12, a small molecule partial agonist CCX662, an extracellular Fab, and an intracellular Fab Method: EM (single particle) / Resolution: 3.3 Å 25177 7sk9 EMDB-25177, PDB-7sk9: Cryo-EM structure of human ACKR3 in complex with a small molecule partial agonist CCX662, and an intracellular Fab Method: EM (single particle) / Resolution: 3.7 Å
Chemicals	ChemComp-CLR: CHOLESTEROL / Cholesterol ChemComp-GJ9: (1R)-4-[7-(3-carboxypropoxy)-6-methylquinolin-8-yl]-1-{[2-(4-hydroxypiperidin-1-yl)-1,3-thiazol-4-yl]methyl}-1,4-diazepan-1-ium ChemComp-LMN: Lauryl Maltose Neopentyl Glycol / detergent*YM
Source	homo sapiens (human) lama glama (llama)
Keywords	SIGNALING PROTEIN/IMMUNE SYSTEM / Atypical Chemokine Receptor / MEMBRANE PROTEIN / SIGNALING PROTEIN / SIGNALING PROTEIN-IMMUNE SYSTEM complex