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	Phosphoantigen-induced inside-out stabilization of butyrophilin receptor complexes drives dimerization-dependent γδ TCR activation.
Journal, issue, pages	Immunity, Vol. 58, Issue 7, Page 1646-11659.e5, Year 2025
Publish date	Jul 8, 2025
Authors	Yuwei Zhu / Wenbo Gao / Jianlin Zheng / Ye Bai / Xinyu Tian / Tengjin Huang / Zebin Lu / De Dong / Anqi Zhang / Changyou Guo / Zhiwei Huang /
PubMed Abstract	Phosphoantigens (pAgs), produced by infected or cancer cells, trigger the assembly of a membrane receptor complex comprising butyrophilin (BTN) members BTN3A1 and BTN2A1, leading to the activation of ...Phosphoantigens (pAgs), produced by infected or cancer cells, trigger the assembly of a membrane receptor complex comprising butyrophilin (BTN) members BTN3A1 and BTN2A1, leading to the activation of γδ T cells. BTN3A2 or BTN3A3 forms heteromers with BTN3A1, exhibiting higher γδ T cell receptor (TCR)-stimulating activity than BTN3A1 homomers. Cryoelectron microscopy (cryo-EM) structure reveals a pAg-induced BTN2A1-BTN3A1 heterotetramer with a 2:2 stoichiometry, stabilized by interactions between the intracellular B30.2 domains and the extracellular immunoglobulin V (IgV) domains. BTN3A2 or BTN3A3 heterodimerizes with BTN3A1, forming a pAg-induced tetrameric complex with BTN2A1. However, BTN3A1 heterodimers are more stable than BTN3A1 homodimers in this interaction. Cryo-EM reveals that BTN2A1-BTN3A1-BTN3A2 binds two γδ TCR ectodomains, with one being sandwiched between the IgV domains of BTN2A1 and BTN3A2, while the other interacts with the free BTN2A1 IgV in the complex, as evidenced by functional data. Together, our findings uncover the mechanism of ligand-induced inside-out stabilization of BTN receptor complexes for dimeric activation of γδ TCR.
External links	Immunity / PubMed:40334665
Methods	EM (single particle)
Resolution	2.9 - 6.95 Å
Structure data	39874 8za6 EMDB-39874, PDB-8za6: Cryo-EM structure of the gdTCR-CD3 complex Method: EM (single particle) / Resolution: 3.43 Å 39875 8za9 EMDB-39875, PDB-8za9: Cryo-EM structure of HBMBPP-BTN2A1-BTN3A1 complex Method: EM (single particle) / Resolution: 3.7 Å 39876 8zaa EMDB-39876, PDB-8zaa: Cryo-EM structure of intracellular HBMBPP-BTN2A1-BTN3A1 complex Method: EM (single particle) / Resolution: 3.46 Å 39877 8zab EMDB-39877, PDB-8zab: Cryo-EM structure of ectodomains of HBMBPP-BTN2A1-BTN3A1 complex Method: EM (single particle) / Resolution: 3.67 Å 39950 8zd4 EMDB-39950, PDB-8zd4: Cryo-EM structure of the gdTCR-ECD Method: EM (single particle) / Resolution: 2.9 Å EMDB-60027: Cryo-EM structure of the Vg9Vd2 TCR-CD3 Method: EM (single particle) / Resolution: 6.95 Å 60577 8zyr EMDB-60577, PDB-8zyr: Cryo-EM structure of BTN2A1-BTN3A1-BTN3A3 Method: EM (single particle) / Resolution: 4.07 Å 60591 9ii6 EMDB-60591, PDB-9ii6: Cryo-EM structure of the intracellular domains of BTN2A1-BTN3A1-BTN3A3 Method: EM (single particle) / Resolution: 3.27 Å 60596 9iik EMDB-60596, PDB-9iik: Cryo-EM structure of BTN2A1-BTN3A1-BTN3A2 Method: EM (single particle) / Resolution: 4.12 Å 61143 9j5j EMDB-61143, PDB-9j5j: Cryo-EM structure of BTN2A1-BTN3A1-BTN3A2 in complex with gdTCR Method: EM (single particle) / Resolution: 4.05 Å 61146 9j5m EMDB-61146, PDB-9j5m: Cryo-EM structure of the ectodomain of BTN2A1-BTN3A1-BTN3A2 in complex with gdTCR Method: EM (single particle) / Resolution: 3.94 Å
Chemicals	ChemComp-CLR: CHOLESTEROL ChemComp-H6P: (2E)-4-hydroxy-3-methylbut-2-en-1-yl trihydrogen diphosphate ChemComp-EIP: 4-HYDROXY-3-METHYL BUTYL DIPHOSPHATE
Source	homo sapiens (human)
Keywords	IMMUNE SYSTEM / complex / immune / protein