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 visualization of small molecule recognition by CXCR3 uncovers dual-agonism in the CXCR3-CXCR7 system.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 3047, Year 2025
Publish date	Mar 28, 2025
Authors	Shirsha Saha / Fumiya K Sano / Saloni Sharma / Manisankar Ganguly / Annu Dalal / Sudha Mishra / Divyanshu Tiwari / Hiroaki Akasaka / Takaaki A Kobayashi / Nabarun Roy / Nashrah Zaidi / Yuzuru Itoh / Rob Leurs / Ramanuj Banerjee / Wataru Shihoya / Osamu Nureki / Arun K Shukla /
PubMed Abstract	Chemokine receptors are critically involved in multiple physiological and pathophysiological processes related to immune response mechanisms. Most chemokine receptors are prototypical GPCRs although ...Chemokine receptors are critically involved in multiple physiological and pathophysiological processes related to immune response mechanisms. Most chemokine receptors are prototypical GPCRs although some also exhibit naturally-encoded signaling-bias toward β-arrestins (βarrs). C-X-C type chemokine receptors, namely CXCR3 and CXCR7, constitute a pair wherein the former is a prototypical GPCR while the latter exhibits selective coupling to βarrs despite sharing a common natural agonist: CXCL11. Moreover, CXCR3 and CXCR7 also recognize small molecule agonists suggesting a modular orthosteric ligand binding pocket. Here, we determine cryo-EM structures of CXCR3 in an Apo-state and in complex with small molecule agonists biased toward G-proteins or βarrs. These structural snapshots uncover an allosteric network bridging the ligand-binding pocket to intracellular side, driving the transducer-coupling bias at this receptor. Furthermore, structural topology of the orthosteric binding pocket also allows us to discover and validate that selected small molecule agonists of CXCR3 display robust agonism at CXCR7. Collectively, our study offers molecular insights into signaling-bias and dual agonism in the CXCR3-CXCR7 system with therapeutic implications.
External links	Nat Commun / PubMed:40155369 / PubMed Central
Methods	EM (single particle)
Resolution	3.03 - 3.68 Å
Structure data	38765 8xxy EMDB-38765, PDB-8xxy: Structure of CXCR3 in the apo-state (Receptor focused map) Method: EM (single particle) / Resolution: 3.68 Å 38766 8xxz EMDB-38766, PDB-8xxz: Structure of CXCR3 in the apo-state (Full map) Method: EM (single particle) / Resolution: 3.3 Å 38774 8xyi EMDB-38774, PDB-8xyi: Structure of CXCR3 in complex with VUF10661 (Receptor-ligand focused map) Method: EM (single particle) / Resolution: 3.16 Å 38776 8xyk EMDB-38776, PDB-8xyk: Structure of CXCR3 in complex with VUF10661 and Go (Full map) Method: EM (single particle) / Resolution: 3.03 Å 38803 8y0h EMDB-38803, PDB-8y0h: Structure of CXCR3 in complex with VUF11418 (Receptor-ligand focused map) Method: EM (single particle) / Resolution: 3.53 Å 38809 8y0n EMDB-38809, PDB-8y0n: Structure of CXCR3 in complex with VUF11418 and Go (Full map) Method: EM (single particle) / Resolution: 3.07 Å
Chemicals	PDB-1lw1: Crystal Structure Of Mycobacterium Tuberculosis Alkylperoxidase Ahpd H137F mutant PDB-1lw2: CRYSTAL STRUCTURE OF T215Y MUTANT HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH 1051U91
Source	homo sapiens (human) mus musculus (house mouse)
Keywords	SIGNALING PROTEIN / GPCR / Arrestin / SIGNALING PROTEIN/IMMUNE / SIGNALING PROTEIN-IMMUNE SYSTEM complex / SIGNALING PROTEIN-IMMUNE complex / SIGNALING PROTEIN/IMMUNE SYSTEM