+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-18900 | |||||||||
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Title | Mouse teneurin-3 non-compact subunit - A0B1 isoform | |||||||||
Map data | Map of mouse teneurin-3 A0B1 isoform ectodomain non-compact subunit | |||||||||
Sample |
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Keywords | Synaptic cell adhesion molecule / Homodimer / Cis-synaptic / CELL ADHESION | |||||||||
Biological species | Mus musculus (house mouse) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
Authors | Gogou C / Meijer DH | |||||||||
Funding support | Netherlands, 1 items
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Citation | Journal: Nat Commun / Year: 2024 Title: Alternative splicing controls teneurin-3 compact dimer formation for neuronal recognition. Authors: Christos Gogou / J Wouter Beugelink / Cátia P Frias / Leanid Kresik / Natalia Jaroszynska / Uwe Drescher / Bert J C Janssen / Robert Hindges / Dimphna H Meijer / Abstract: Neuronal network formation is facilitated by recognition between synaptic cell adhesion molecules at the cell surface. Alternative splicing of cell adhesion molecules provides additional specificity ...Neuronal network formation is facilitated by recognition between synaptic cell adhesion molecules at the cell surface. Alternative splicing of cell adhesion molecules provides additional specificity in forming neuronal connections. For the teneurin family of cell adhesion molecules, alternative splicing of the EGF-repeats and NHL domain controls synaptic protein-protein interactions. Here we present cryo-EM structures of the compact dimeric ectodomain of two teneurin-3 isoforms that harbour the splice insert in the EGF-repeats. This dimer is stabilised by an EGF8-ABD contact between subunits. Cryo-EM reconstructions of all four splice variants, together with SAXS and negative stain EM, reveal compacted dimers for each, with variant-specific dimeric arrangements. This results in specific trans-cellular interactions, as tested in cell clustering and stripe assays. The compact conformations provide a structural basis for teneurin homo- and heterophilic interactions. Altogether, our findings demonstrate how alternative splicing results in rearrangements of the dimeric subunits, influencing neuronal recognition and likely circuit wiring. #1: Journal: BioRxiv Title: Mouse teneurin-3 non-compact subunit - A0B1 isoform Authors: Gogou C / Meijer DH | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_18900.map.gz | 78.5 MB | EMDB map data format | |
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Header (meta data) | emd-18900-v30.xml emd-18900.xml | 14.5 KB 14.5 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_18900_fsc.xml | 10 KB | Display | FSC data file |
Images | emd_18900.png | 108.6 KB | ||
Filedesc metadata | emd-18900.cif.gz | 4.1 KB | ||
Others | emd_18900_half_map_1.map.gz emd_18900_half_map_2.map.gz | 65.5 MB 65.6 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-18900 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-18900 | HTTPS FTP |
-Validation report
Summary document | emd_18900_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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Full document | emd_18900_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | emd_18900_validation.xml.gz | 17.1 KB | Display | |
Data in CIF | emd_18900_validation.cif.gz | 22.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18900 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-18900 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_18900.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Annotation | Map of mouse teneurin-3 A0B1 isoform ectodomain non-compact subunit | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.836 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Half map of mouse teneurin-3 A0B1 isoform ectodomain...
File | emd_18900_half_map_1.map | ||||||||||||
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Annotation | Half map of mouse teneurin-3 A0B1 isoform ectodomain non-compact subunit | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map of mouse teneurin-3 A0B1 isoform ectodomain...
File | emd_18900_half_map_2.map | ||||||||||||
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Annotation | Half map of mouse teneurin-3 A0B1 isoform ectodomain non-compact subunit | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : mouse teneurin-3 A1B1 isoform ectodomain subunit
Entire | Name: mouse teneurin-3 A1B1 isoform ectodomain subunit |
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Components |
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-Supramolecule #1: mouse teneurin-3 A1B1 isoform ectodomain subunit
Supramolecule | Name: mouse teneurin-3 A1B1 isoform ectodomain subunit / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: Mus musculus (house mouse) |
Molecular weight | Theoretical: 536.96 KDa |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 0.5 mg/mL |
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Buffer | pH: 7.8 / Details: 20 mM HEPES, 150 mM NaCl, 2mM CaCl2 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 295 K |
-Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (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: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |