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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Pentagonal cluster of BAFF-TACI ectodomain complex | |||||||||
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Sample |
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Keywords | TNF receptor family / Receptor / Receptor cluster / IMMUNE SYSTEM | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.95 Å | |||||||||
Authors | Lim CS / Lee JO | |||||||||
| Funding support | Korea, Republic Of, 1 items
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Citation | Journal: Nat Commun / Year: 2025Title: 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. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_63177.map.gz | 167.8 MB | EMDB map data format | |
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| Header (meta data) | emd-63177-v30.xml emd-63177.xml | 14.4 KB 14.4 KB | Display Display | EMDB header |
| Images | emd_63177.png | 105.1 KB | ||
| Masks | emd_63177_msk_1.map | 178 MB | Mask map | |
| Filedesc metadata | emd-63177.cif.gz | 4.2 KB | ||
| Others | emd_63177_half_map_1.map.gz emd_63177_half_map_2.map.gz | 165.3 MB 165.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-63177 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-63177 | HTTPS FTP |
-Validation report
| Summary document | emd_63177_validation.pdf.gz | 852.1 KB | Display | EMDB validaton report |
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| Full document | emd_63177_full_validation.pdf.gz | 851.7 KB | Display | |
| Data in XML | emd_63177_validation.xml.gz | 15.1 KB | Display | |
| Data in CIF | emd_63177_validation.cif.gz | 18 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-63177 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-63177 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_63177.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
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| Voxel size | X=Y=Z: 0.82 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_63177_msk_1.map | ||||||||||||
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-Half map: #1
| File | emd_63177_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_63177_half_map_2.map | ||||||||||||
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Sample components
-Entire : Pentagonal cluster of BAFF-TACI ectodomain 3:3 complex
| Entire | Name: Pentagonal cluster of BAFF-TACI ectodomain 3:3 complex |
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| Components |
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-Supramolecule #1: Pentagonal cluster of BAFF-TACI ectodomain 3:3 complex
| Supramolecule | Name: Pentagonal cluster of BAFF-TACI ectodomain 3:3 complex type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.1 mg/mL | |||||||||
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| Buffer | pH: 7.8 Component:
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| Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY | |||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 293 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 105000 |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | PDB ID: Chain - Source name: PDB / Chain - Initial model type: experimental model |
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| Refinement | Protocol: RIGID BODY FIT |
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
Korea, Republic Of, 1 items
Citation
















Z (Sec.)
Y (Row.)
X (Col.)












































FIELD EMISSION GUN

