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- EMDB-60488: Cluster structure of BAFF-BAFFR-TRAF3(His) complex -

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Basic information

Entry
Database: EMDB / ID: EMD-60488
TitleCluster structure of BAFF-BAFFR-TRAF3(His) complex
Map data
Sample
  • Complex: Cluster structure of the BAFF-BAFFR-TRAF3(His) complex
    • Protein or peptide: Chains: A,B,C,G,H,I,M,N,O,S,T,U,Y,Z,a,e,f,g,k,l,m
    • Protein or peptide: Chains: D,E,F,J,K,L,P,Q,R,V,W,X,b,c,d,h,i,j,n,o,p
KeywordsReceptor cluster / Signal complex / membrane receptor / IMMUNE SYSTEM
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.77 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_60488.png

Downloads & links

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Map

FileDownload / File: emd_60488.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.
= 435.2 Å		1.09 Å/pix.
x 400 pix.
= 435.2 Å		1.09 Å/pix.
x 400 pix.
= 435.2 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: 0.7
Minimum - Maximum-2.4271677 - 3.6074162
Average (Standard dev.)0.0011312871 (±0.06861189)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 435.2 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_60488_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_60488_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : Cluster structure of the BAFF-BAFFR-TRAF3(His) complex

EntireName: Cluster structure of the BAFF-BAFFR-TRAF3(His) complex
Components
  • Complex: Cluster structure of the BAFF-BAFFR-TRAF3(His) complex
    • Protein or peptide: Chains: A,B,C,G,H,I,M,N,O,S,T,U,Y,Z,a,e,f,g,k,l,m
    • Protein or peptide: Chains: D,E,F,J,K,L,P,Q,R,V,W,X,b,c,d,h,i,j,n,o,p

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Supramolecule #1: Cluster structure of the BAFF-BAFFR-TRAF3(His) complex

SupramoleculeName: Cluster structure of the BAFF-BAFFR-TRAF3(His) 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,M,N,O,S,T,U,Y,Z,a,e,f,g,k,l,m

MacromoleculeName: Chains: A,B,C,G,H,I,M,N,O,S,T,U,Y,Z,a,e,f,g,k,l,m / type: protein_or_peptide / ID: 1 / Details: TRAF3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MHHHHHHHHG GGGSKNDGSG GGGSNTGLLE SQLSRHDQML SVHDIRLADM DLRFQVLETA SYNGVLIWKI RDYKRRKQEA VMGKTLSLYS QPFYTGYFGY KMCARVYLNG DGMGKGTHLS LFFVIMRGEY DALLPWPFKQ KVTLMLMDQG SSRRHLGDAF KPDPNSSSFK ...String:
MHHHHHHHHG GGGSKNDGSG GGGSNTGLLE SQLSRHDQML SVHDIRLADM DLRFQVLETA SYNGVLIWKI RDYKRRKQEA VMGKTLSLYS QPFYTGYFGY KMCARVYLNG DGMGKGTHLS LFFVIMRGEY DALLPWPFKQ KVTLMLMDQG SSRRHLGDAF KPDPNSSSFK KPTGEMNIAS GCPVFVAQTV LENGTYIKDD TIFIKVIVDT SDLPDPGGSL VPR

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Macromolecule #2: Chains: D,E,F,J,K,L,P,Q,R,V,W,X,b,c,d,h,i,j,n,o,p

MacromoleculeName: Chains: D,E,F,J,K,L,P,Q,R,V,W,X,b,c,d,h,i,j,n,o,p / type: protein_or_peptide / ID: 2 / Details: BAFFR / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MRRGPRSLRG RDAPAPTPCV PAECFDLLVR HCVACGLLRT PRPKPAGASS PAPRTALQPQ ESVGAGAGEA ALPLPGLLFG APALLGLAL VLALVLVGLV SWRRRQRRLR GASSAEAPDG DKDAPEPLDK VIILSPGISD ATAPAWPPPG EDPGTTPPGH S VPVPATEL ...String:
MRRGPRSLRG RDAPAPTPCV PAECFDLLVR HCVACGLLRT PRPKPAGASS PAPRTALQPQ ESVGAGAGEA ALPLPGLLFG APALLGLAL VLALVLVGLV SWRRRQRRLR GASSAEAPDG DKDAPEPLDK VIILSPGISD ATAPAWPPPG EDPGTTPPGH S VPVPATEL GSTELVTTKT AGPEQQSNSL 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: 40.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Final reconstructionApplied symmetry - Point group: C3 (3 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.77 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 493981
Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER

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