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- EMDB-60490: Binary cluster of TNF-TNFR1 full-length complex -

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Basic information

Entry
Database: EMDB / ID: EMD-60490
TitleBinary cluster of TNF-TNFR1 full-length complex
Map data
Sample
  • Complex: Binary cluster of TNF-TNFR1 3:3 complex
    • Protein or peptide: Chains: A,B,C,G,H,I
    • Protein or peptide: Chains: D,E,F,J,K,L
KeywordsTNF receptor / Receptor / Receptor cluster / IMMUNE SYSTEM
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 6.02 Å
AuthorsLim CS / Lee JO
Funding support Korea, Republic Of, 1 items
OrganizationGrant numberCountry
Other government Korea, Republic Of
CitationJournal: Nat Commun / Year: 2025
Title: Highly ordered clustering of TNFα and BAFF ligand-receptor-intracellular adaptor complexes on a lipid membrane.
Authors: Chan Seok Lim / Jisun Lee / Ji Won Kim / Jie-Oh Lee /
Abstract: The TNF family plays a critical role in immune regulation. Here, we present high-resolution structures of clusters formed by two TNF receptor family proteins, TNFR1 and BAFFR. Using a lipid monolayer ...The TNF family plays a critical role in immune regulation. Here, we present high-resolution structures of clusters formed by two TNF receptor family proteins, TNFR1 and BAFFR. Using a lipid monolayer method to mimic their membrane-bound state, we observe that the TNFα-TNFR1 complex forms highly ordered clusters of trimers on the lipid membrane. A non-competitive TNFR1 antagonist that inhibits receptor activation disrupted these clusters without blocking ligand binding or receptor trimerization. Furthermore, we find that the BAFF-BAFFR, BAFF-TACI, and BAFF-BCMA receptor-ligand complexes predominantly form pentagonal clusters of trimers on the lipid membrane. Notably, the binding of the intracellular adaptor TRAF3 to the BAFF-BAFFR complex induces a structural transition from a pentagonal to a flat hexagonal cluster. Mutations in BAFF that impair BAFFR activation prevented cluster formation. Our findings demonstrate that ligand binding induces the formation of highly ordered clusters of TNFR1 and BAFFR receptors on the lipid membrane, which is essential for their activation.
History
DepositionJun 9, 2024-
Header (metadata) releaseJun 11, 2025-
Map releaseJun 11, 2025-
UpdateAug 6, 2025-
Current statusAug 6, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_60490.png

Downloads & links

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Map

FileDownload / File: emd_60490.map.gz / Format: CCP4 / Size: 103 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 300 pix.
= 326.4 Å		1.09 Å/pix.
x 300 pix.
= 326.4 Å		1.09 Å/pix.
x 300 pix.
= 326.4 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.088 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.284
Minimum - Maximum-1.6113445 - 1.9104702
Average (Standard dev.)-0.0008207114 (±0.055782)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 326.40002 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_60490_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_60490_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Binary cluster of TNF-TNFR1 3:3 complex

EntireName: Binary cluster of TNF-TNFR1 3:3 complex
Components
  • Complex: Binary cluster of TNF-TNFR1 3:3 complex
    • Protein or peptide: Chains: A,B,C,G,H,I
    • Protein or peptide: Chains: D,E,F,J,K,L

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Supramolecule #1: Binary cluster of TNF-TNFR1 3:3 complex

SupramoleculeName: Binary cluster of TNF-TNFR1 3:3 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Chains: A,B,C,G,H,I

MacromoleculeName: Chains: A,B,C,G,H,I / type: protein_or_peptide / ID: 1 / Details: TNF ligand / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
ADPVRSSSRT PSDKPVAHVV ANPQAEGQLQ WLNRRANALL ANGVELRDNQ LVVPSEGLYL IYSQVLFKGQ GCPSTHVLLT HTISRIAVSY QTKVNLLSAI KSPCQRETPE GAEAKPWYEP IYLGGVFQLE KGDRLSAEIN RPDYLDFAES GQVYFGIIAL EFRSGRLVPR GSHHHHHH

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Macromolecule #2: Chains: D,E,F,J,K,L

MacromoleculeName: Chains: D,E,F,J,K,L / type: protein_or_peptide / ID: 2 / Details: TNFR1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: LVPHLGDREK RDSVCPQGKY IHPQNNSICC TKCHKGTYLY NDCPGPGQDT DCRECESGSF TASENHLRHC LSCSKCRKEM GQVEISSCTV DRDTVCGCRK NQYRHYWSEN LFQCFNCSLC LNGTVHLSCQ EKQNTVCTCH AGFFLRENEC VSCSNCKKSL ECTKLCLPQI ...String:
LVPHLGDREK RDSVCPQGKY IHPQNNSICC TKCHKGTYLY NDCPGPGQDT DCRECESGSF TASENHLRHC LSCSKCRKEM GQVEISSCTV DRDTVCGCRK NQYRHYWSEN LFQCFNCSLC LNGTVHLSCQ EKQNTVCTCH AGFFLRENEC VSCSNCKKSL ECTKLCLPQI ENVKGTEDSG TTVLLPLVIF FGLCLLSLLF IGLMYRYQRW KSKLYSIVCG KSTPEKEGEL EGTTTKPLAP NPSFSPTPGF TPTLGFSPVP SSTFTSSSTY TPGDCPNFAA PRREVAPPYQ GADPILATAL ASDPIPNPLQ KWEDSAHKPQ SLDTDDPATL YAVVENVPPL RWKEFVRRLG LSDHEIDRLE LQNGRCLREA QYSMLATWRR RTPRREATLE LLGRVLRDMD LLGCLEDIEE ALCGPAALPP APSLLRSNSL EVLFQ

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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: 7.8
Component:
ConcentrationFormulaName
20.0 mMC4H11NO3Tris
150.0 mMNaClSodium chloride
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 293 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 45.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.2 µm

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Final reconstructionApplied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 6.02 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 12412
Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER

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