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 complete extracellular receptor assemblies mediated by IL-12 and IL-23.
Journal, issue, pages	Nat Struct Mol Biol, Vol. 31, Issue 4, Page 591-597, Year 2024
Publish date	Jan 29, 2024
Authors	Yehudi Bloch / Jan Felix / Romain Merceron / Mathias Provost / Royan Alipour Symakani / Robin De Backer / Elisabeth Lambert / Ahmad R Mehdipour / Savvas N Savvides /
PubMed Abstract	Cell-surface receptor complexes mediated by pro-inflammatory interleukin (IL)-12 and IL-23, both validated therapeutic targets, are incompletely understood due to the lack of structural insights into ...Cell-surface receptor complexes mediated by pro-inflammatory interleukin (IL)-12 and IL-23, both validated therapeutic targets, are incompletely understood due to the lack of structural insights into their complete extracellular assemblies. Furthermore, there is a paucity of structural details describing the IL-12-receptor interaction interfaces, in contrast to IL-23-receptor complexes. Here we report structures of fully assembled mouse IL-12/human IL-23-receptor complexes comprising the complete extracellular segments of the cognate receptors determined by electron cryo-microscopy. The structures reveal key commonalities but also surprisingly diverse features. Most notably, whereas IL-12 and IL-23 both utilize a conspicuously presented aromatic residue on their α-subunit as a hotspot to interact with the N-terminal Ig domain of their high-affinity receptors, only IL-12 juxtaposes receptor domains proximal to the cell membrane. Collectively, our findings will help to complete our understanding of cytokine-mediated assemblies of tall cytokine receptors and will enable a cytokine-specific interrogation of IL-12/IL-23 signaling in physiology and disease.
External links	Nat Struct Mol Biol / PubMed:38287195
Methods	EM (single particle) / X-ray diffraction
Resolution	2 - 6.7 Å
Structure data	16820 8odz EMDB-16820, PDB-8odz: Cryo-EM structure of a pre-dimerized murine IL-12 complete extracellular signaling complex (Class 1). Method: EM (single particle) / Resolution: 3.6 Å 16821 8oe0 EMDB-16821, PDB-8oe0: Cryo-EM structure of a pre-dimerized murine IL-12 complete extracellular signaling complex (Class 2). Method: EM (single particle) / Resolution: 4.6 Å EMDB-16822: Cryo-EM structure of the murine IL-12 complete extracellular signaling complex (Class 1). Method: EM (single particle) / Resolution: 5.6 Å EMDB-16823: Cryo-EM structure of the murine IL-12 complete extracellular signaling complex (Class 2). Method: EM (single particle) / Resolution: 6.7 Å 16824 8oe4 EMDB-16824, PDB-8oe4: Cryo-EM structure of a pre-dimerized human IL-23 complete extracellular signaling complex. Method: EM (single particle) / Resolution: 3.6 Å 17580 8pb1 EMDB-17580, PDB-8pb1: Cryo-EM structure of a pre-dimerized murine IL-12 complete extracellular signaling complex (Class 1), obtained after local refinement. Method: EM (single particle) / Resolution: 3.5 Å PDB-8c7m: Interleukin 12 receptor subunit beta-1 Fn domains in complex with antagonistic FAb fragment. Method: X-RAY DIFFRACTION / Resolution: 2.56 Å PDB-8cr5: Murine Interleukin-12 receptor beta 1 domain 1 in complex with murine Interleukin-12 beta. Method: X-RAY DIFFRACTION / Resolution: 2.15 Å PDB-8cr6: mouse Interleukin-12 Method: X-RAY DIFFRACTION / Resolution: 2.85 Å PDB-8cr8: human Interleukin-23 Method: X-RAY DIFFRACTION / Resolution: 2 Å PDB-8odx: Interleukin 12 receptor subunit beta-1 Fn domains in complex with antagonistic FAb4 fragment and VHH. Method: X-RAY DIFFRACTION / Resolution: 4.4 Å PDB-8ppm: IL-12Rb1 neutralizing Fab4, crystal kappa variant Method: X-RAY DIFFRACTION / Resolution: 2.03 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-CL: Unknown entry ChemComp-HOH: WATER ChemComp-TB: TERBIUM(III) ION ChemComp-K: Unknown entry
Source	mus musculus (house mouse) homo sapiens (human) homo sapiens x mus musculus hybrid cell line (mammal) lama glama (llama)
Keywords	CYTOKINE / receptor / antagonist / antibody / complex / inflammation / glycoprotein / immunity / heterodimer / EXTRACELLULAR / FIBRONECTIN TYPE III / fibronectin / SIGNALING PROTEIN / IMMUNOSUPPRESSANT / Fab fragment / designed crystal contact