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- EMDB-60161: Cryo-EM structure of the full-length pAg-bound BTN2A1-BTN3A1-BTN3... -

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Basic information

Entry
Database: EMDB / ID: EMD-60161
TitleCryo-EM structure of the full-length pAg-bound BTN2A1-BTN3A1-BTN3A3 complex
Map data
Sample
  • Complex: Human BTN complex
    • Protein or peptide: Butyrophilin subfamily 2 member A1
    • Protein or peptide: Butyrophilin subfamily 3 member A3
    • Protein or peptide: Butyrophilin subfamily 3 member A1
  • Ligand: (2E)-4-hydroxy-3-methylbut-2-en-1-yl trihydrogen diphosphate
KeywordsReceptor / IMMUNE SYSTEM
Function / homology
Function and homology information


activated T cell proliferation / Butyrophilin (BTN) family interactions / T cell mediated immunity / lipid metabolic process / regulation of cytokine production / positive regulation of cytokine production / positive regulation of type II interferon production / T cell receptor signaling pathway / external side of plasma membrane / signaling receptor binding ...activated T cell proliferation / Butyrophilin (BTN) family interactions / T cell mediated immunity / lipid metabolic process / regulation of cytokine production / positive regulation of cytokine production / positive regulation of type II interferon production / T cell receptor signaling pathway / external side of plasma membrane / signaling receptor binding / membrane / plasma membrane
Similarity search - Function
Butyrophilin subfamily 1/2, SPRY/PRY domain / Butyrophilin subfamily 3, PRY/SPRY domain / : / : / Butyrophilin subfamily 3 member A2-like, Ig-C domain / SPRY-associated domain / SPRY-associated / PRY / Butyrophylin-like, SPRY domain / SPRY domain ...Butyrophilin subfamily 1/2, SPRY/PRY domain / Butyrophilin subfamily 3, PRY/SPRY domain / : / : / Butyrophilin subfamily 3 member A2-like, Ig-C domain / SPRY-associated domain / SPRY-associated / PRY / Butyrophylin-like, SPRY domain / SPRY domain / B30.2/SPRY domain / B30.2/SPRY domain profile. / B30.2/SPRY domain superfamily / Domain in SPla and the RYanodine Receptor. / SPRY domain / Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Immunoglobulin subtype / Immunoglobulin / Concanavalin A-like lectin/glucanase domain superfamily / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
Butyrophilin subfamily 3 member A3 / Butyrophilin subfamily 3 member A1 / Butyrophilin subfamily 2 member A1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsXin W / Huang B / Su Q / Zhou Q
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32100975 China
Citation
Journal: Cell Discov / Year: 2026
Title: Phosphoantigen-driven dissociation of butyrophilin oligomers activates γδ T cells.
Authors: Weizhi Xin / Bangdong Huang / Weijie Gao / Wenjia Zhang / Yundi Hu / Yuehua Liu / Enyuan Liang / Jin Chen / Yigong Shi / Qiang Su / Qiang Zhou /
Abstract: γδ T cells represent a promising avenue for cancer immunotherapy. The Vγ9Vδ2 T-cell receptor (TCR), which is expressed by the predominant subset of γδ T cells, responds to phosphoantigen (pAg)- ...γδ T cells represent a promising avenue for cancer immunotherapy. The Vγ9Vδ2 T-cell receptor (TCR), which is expressed by the predominant subset of γδ T cells, responds to phosphoantigen (pAg)-engaged butyrophilins (BTNs) on various cancer cells. However, the molecular mechanism underlying the pAg-mediated activation of Vγ9Vδ2 TCRs remains a subject of debate. Here, we employed an integrative approach to elucidate the mechanism of pAg reactivity in Vγ9Vδ2 T cells. Our results demonstrate that BTNs form higher-order oligomers in the absence of pAg. Upon pAg binding, these higher-order oligomers dissociate into separate tetramers, enabling Vγ9Vδ2 TCR engagement. This pAg-induced dissociation of higher-order BTN oligomers is critical for pAg-mediated activation of γδ T cells. Our findings reveal a mechanism of BTN higher-order oligomer dissociation-driven pAg sensing, providing valuable insight for future immunotherapeutic strategies.
#1: Journal: Biorxiv / Year: 2025
Title: Phosphoantigen-Driven Dissociation of Butyrophilin Oligomers Activates gamma delta T Cells
Authors: Xin W / Huang B / Gao W / Zhang W / Hu Y / Liu Y / Liang E / Shi Y / Su Q / Zhou Q
History
DepositionMay 15, 2024-
Header (metadata) releaseNov 26, 2025-
Map releaseNov 26, 2025-
UpdateSep 30, 2026-
Current statusSep 30, 2026Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_60161.png

Downloads & links

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Map

FileDownload / File: emd_60161.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.09 Å/pix.
x 400 pix.
= 434.8 Å		1.09 Å/pix.
x 400 pix.
= 434.8 Å		1.09 Å/pix.
x 400 pix.
= 434.8 Å

Surface

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Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.087 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0028
Minimum - Maximum-0.0088294735 - 0.025367834
Average (Standard dev.)-0.000016095632 (±0.00056820695)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 434.80002 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_60161_msk_1.map
Projections & Slices
AxesZYX

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Histogram (log scale)

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Half map: #2

Fileemd_60161_half_map_1.map
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Half map: #1

Fileemd_60161_half_map_2.map
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Sample components

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Entire : Human BTN complex

EntireName: Human BTN complex
Components
  • Complex: Human BTN complex
    • Protein or peptide: Butyrophilin subfamily 2 member A1
    • Protein or peptide: Butyrophilin subfamily 3 member A3
    • Protein or peptide: Butyrophilin subfamily 3 member A1
  • Ligand: (2E)-4-hydroxy-3-methylbut-2-en-1-yl trihydrogen diphosphate

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Supramolecule #1: Human BTN complex

SupramoleculeName: Human BTN complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 213 kDa/nm

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Macromolecule #1: Butyrophilin subfamily 2 member A1

MacromoleculeName: Butyrophilin subfamily 2 member A1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 56.074164 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: FIVVGPTDPI LATVGENTTL RCHLSPEKNA EDMEVRWFRS QFSPAVFVYK GGRERTEEQM EEYRGRTTFV SKDISRGSVA LVIHNITAQ ENGTYRCYFQ EGRSYDEAIL HLVVAGLGSK PLISMRGHED GGIRLECISR GWYPKPLTVW RDPYGGVAPA L KEVSMPDA ...String:
FIVVGPTDPI LATVGENTTL RCHLSPEKNA EDMEVRWFRS QFSPAVFVYK GGRERTEEQM EEYRGRTTFV SKDISRGSVA LVIHNITAQ ENGTYRCYFQ EGRSYDEAIL HLVVAGLGSK PLISMRGHED GGIRLECISR GWYPKPLTVW RDPYGGVAPA L KEVSMPDA DGLFMVTTAV IIRDKSVRNM SCSINNTLLG QKKESVIFIP ESFMPSVSPC AVALPIIVVI LMIPIAVCIY WI NKLQKEK KILSGEKEFE RETREIALKE LEKERVQKEE ELQVKEKLQE ELRWRRTFLH AVDVVLDPDT AHPDLFLSED RRS VRRCPF RHLGESVPDN PERFDSQPCV LGRESFASGK HYWEVEVENV IEWTVGVCRD SVERKGEVLL IPQNGFWTLE MHKG QYRAV SSPDRILPLK ESLCRVGVFL DYEAGDVSFY NMRDRSHIYT CPRSAFSVPV RPFFRLGCED SPIFICPALT GANGV TVPE EGLTLHRV

UniProtKB: Butyrophilin subfamily 2 member A1

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Macromolecule #2: Butyrophilin subfamily 3 member A3

MacromoleculeName: Butyrophilin subfamily 3 member A3 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 54.21243 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: QFSVLGPSGP ILAMVGEDAD LPCHLFPTMS AETMELRWVS SSLRQVVNVY ADGKEVEDRQ SAPYRGRTSI LRDGITAGKA ALRIHNVTA SDSGKYLCYF QDGDFYEKAL VELKVAALGS DLHIEVKGYE DGGIHLECRS TGWYPQPQIK WSDTKGENIP A VEAPVVAD ...String:
QFSVLGPSGP ILAMVGEDAD LPCHLFPTMS AETMELRWVS SSLRQVVNVY ADGKEVEDRQ SAPYRGRTSI LRDGITAGKA ALRIHNVTA SDSGKYLCYF QDGDFYEKAL VELKVAALGS DLHIEVKGYE DGGIHLECRS TGWYPQPQIK WSDTKGENIP A VEAPVVAD GVGLYAVAAS VIMRGSSGGG VSCIIRNSLL GLEKTASISI ADPFFRSAQP WIAALAGTLP ISLLLLAGAS YF LWRQQKE KIALSRETER EREMKEMGYA ATEQEISLRE KLQEELKWRK IQYMARGEKS LAYHEWKMAL FKPADVILDP DTA NAILLV SEDQRSVQRA EEPRDLPDNP ERFEWRYCVL GCENFTSGRH YWEVEVGDRK EWHIGVCSKN VERKKGWVKM TPEN GYWTM GLTDGNKYRA LTEPRTNLKL PEPPRKVGIF LDYETGEISF YNATDGSHIY TFPHASFSEP LYPVFRILTL EPTAL TI

UniProtKB: Butyrophilin subfamily 3 member A3

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Macromolecule #3: Butyrophilin subfamily 3 member A1

MacromoleculeName: Butyrophilin subfamily 3 member A1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 54.42882 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: QFSVLGPSGP ILAMVGEDAD LPCHLFPTMS AETMELKWVS SSLRQVVNVY ADGKEVEDRQ SAPYRGRTSI LRDGITAGKA ALRIHNVTA SDSGKYLCYF QDGDFYEKAL VELKVAALGS DLHVDVKGYK DGGIHLECRS TGWYPQPQIQ WSNNKGENIP T VEAPVVAD ...String:
QFSVLGPSGP ILAMVGEDAD LPCHLFPTMS AETMELKWVS SSLRQVVNVY ADGKEVEDRQ SAPYRGRTSI LRDGITAGKA ALRIHNVTA SDSGKYLCYF QDGDFYEKAL VELKVAALGS DLHVDVKGYK DGGIHLECRS TGWYPQPQIQ WSNNKGENIP T VEAPVVAD GVGLYAVAAS VIMRGSSGEG VSCTIRSSLL GLEKTASISI ADPFFRSAQR WIAALAGTLP VLLLLLGGAG YF LWQQQEE KKTQFRKKKR EQELREMAWS TMKQEQSTRV KLLEELRWRS IQYASRGERH SAYNEWKKAL FKPADVILDP KTA NPILLV SEDQRSVQRA KEPQDLPDNP ERFNWHYCVL GCESFISGRH YWEVEVGDRK EWHIGVCSKN VQRKGWVKMT PENG FWTMG LTDGNKYRTL TEPRTNLKLP KPPKKVGVFL DYETGDISFY NAVDGSHIHT FLDVSFSEAL YPVFRILTLE PTALT ICPA

UniProtKB: Butyrophilin subfamily 3 member A1

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Macromolecule #4: (2E)-4-hydroxy-3-methylbut-2-en-1-yl trihydrogen diphosphate

MacromoleculeName: (2E)-4-hydroxy-3-methylbut-2-en-1-yl trihydrogen diphosphate
type: ligand / ID: 4 / Number of copies: 1 / Formula: H6P
Molecular weightTheoretical: 262.092 Da
Chemical component information

ChemComp-H6P:
(2E)-4-hydroxy-3-methylbut-2-en-1-yl trihydrogen diphosphate

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 8962628
CTF correctionSoftware - Name: cryoSPARC (ver. 4.4.1) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 5) / Number images used: 426857
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.4.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.4.1)

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