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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Mouse Teneurin2 dimer variant A1B0 | |||||||||
Map data | DeepEMhancer sharpened map | |||||||||
Sample |
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Keywords | cell adhesion molecule / complex / homodimer / CELL ADHESION | |||||||||
| Function / homology | Function and homology informationfilopodium / PML body / growth cone / presynaptic membrane / dendritic spine / postsynaptic membrane / cell adhesion / Golgi apparatus / signal transduction / endoplasmic reticulum ...filopodium / PML body / growth cone / presynaptic membrane / dendritic spine / postsynaptic membrane / cell adhesion / Golgi apparatus / signal transduction / endoplasmic reticulum / protein homodimerization activity / DNA-templated transcription Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.55 Å | |||||||||
Authors | Berbeira-Santana M / Zhou JC / el Omari K / Baker L / Seiradake E | |||||||||
| Funding support | United Kingdom, 1 items
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Citation | Journal: Nat Commun / Year: 2026Title: Structurally exclusive Teneurin complexes orchestrate divergent programs in early cortical development. Authors: Miguel Berbeira-Santana / Claudia Peregrina / Kosuke Okuda / Jin Chuan Zhou / Maria Carrasquero-Ordaz / Amy V Roberts / Anne E Thomas / Evert Haanappel / Matthieu Chavent / Kamel El Omari / ...Authors: Miguel Berbeira-Santana / Claudia Peregrina / Kosuke Okuda / Jin Chuan Zhou / Maria Carrasquero-Ordaz / Amy V Roberts / Anne E Thomas / Evert Haanappel / Matthieu Chavent / Kamel El Omari / Lindsay A Baker / Daniel T Pederick / Els Pardon / Jan Steyaert / U Valentin Nägerl / Daniel Del Toro / Elena Seiradake / ![]() Abstract: Cortical migration is a complex process in which neurons migrate along radial glial cells (RGC) to form functional layers. Teneurins (Ten1-4) play a role by interacting with Latrophilins (Lphn/ADGRL1- ...Cortical migration is a complex process in which neurons migrate along radial glial cells (RGC) to form functional layers. Teneurins (Ten1-4) play a role by interacting with Latrophilins (Lphn/ADGRL1-3). Teneurins are also known as cell adhesion molecules, but how homophilic and heterophilic Teneurin interactions are integrated is unknown. Here, single-particle-cryo-EM data of Ten2 shows that canonical Latrophilin-binding is sterically incompatible with Ten2-dimerisation, making these interactions exclusive. We engineered surface mutations that specifically disrupt Ten2-Ten2 or Ten2-Latrophilin interactions. These are transferrable to Ten4, suggesting conserved binding mechanisms. Proteomics, in-vivo-gene-editing and super-resolution-microscopy show that Ten4 is expressed along RGC fibres and that migrating neurons switch from low-to-high Ten4-expression. Ten4 expression is highest in the cortical plate where Ten4-Ten4 interactions reduce RGC-attachment. In the intermediate zone, Ten4-Latrophilin interactions are required to promote neuron-RGC association. The results show how Ten4 orchestrates different stages of cortical migration by using a structural/functional switch between high-affinity Lphn interactions and low-affinity homophilic interactions, underpinning the integration of distinct migration programmes. | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_50976.map.gz | 136.2 MB | EMDB map data format | |
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| Header (meta data) | emd-50976-v30.xml emd-50976.xml | 25.7 KB 25.7 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_50976_fsc.xml | 11.5 KB | Display | FSC data file |
| Images | emd_50976.png | 65.4 KB | ||
| Filedesc metadata | emd-50976.cif.gz | 8.6 KB | ||
| Others | emd_50976_additional_1.map.gz emd_50976_half_map_1.map.gz emd_50976_half_map_2.map.gz | 81.9 MB 151.8 MB 151.8 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-50976 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-50976 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9g2hMC ![]() 9g2fC ![]() 9g41C ![]() 9g42C M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_50976.map.gz / Format: CCP4 / Size: 163.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | DeepEMhancer sharpened map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.83 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: Raw map
| File | emd_50976_additional_1.map | ||||||||||||
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| Annotation | Raw map | ||||||||||||
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| Density Histograms |
-Half map: Half map A
| File | emd_50976_half_map_1.map | ||||||||||||
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| Annotation | Half map A | ||||||||||||
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| Density Histograms |
-Half map: Half map B
| File | emd_50976_half_map_2.map | ||||||||||||
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| Annotation | Half map B | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Dimeric complex of mouse Teneurin2 A1B0 variant
| Entire | Name: Dimeric complex of mouse Teneurin2 A1B0 variant |
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| Components |
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-Supramolecule #1: Dimeric complex of mouse Teneurin2 A1B0 variant
| Supramolecule | Name: Dimeric complex of mouse Teneurin2 A1B0 variant / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 Details: Dimeric complex purified by SEC after recombinant expression in HEK293T cells. |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 267.78383 KDa |
-Macromolecule #1: Teneurin transmembrane protein 2
| Macromolecule | Name: Teneurin transmembrane protein 2 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 267.134719 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: ETGHHHHHHR GGLNDIFEAQ KIEWHEGGST GHLLGLNWQL QPADGHTFNN GVRTGLPGND DVATVPSGGK VPWSLKNSSI DSGEAEVGR RVTQEVPPGV FWRSQIHISQ PQFLKFNISL GKDALFGVYI RRGLPPSHAQ YDFMERLDGK EKWSVVESPR E RRSIQTLV ...String: ETGHHHHHHR GGLNDIFEAQ KIEWHEGGST GHLLGLNWQL QPADGHTFNN GVRTGLPGND DVATVPSGGK VPWSLKNSSI DSGEAEVGR RVTQEVPPGV FWRSQIHISQ PQFLKFNISL GKDALFGVYI RRGLPPSHAQ YDFMERLDGK EKWSVVESPR E RRSIQTLV QNEAVFVQYL DVGLWHLAFY NDGKDKEMVS FNTVVLDSVQ DCPRNCHGNG ECVSGLCHCF PGFLGADCAK AA CPVLCSG NGQYSKGTCQ CYSGWKGAEC DVPMNQCIDP SCGGHGSCID GNCVCAAGYK GEHCEEVDCL DPTCSSHGVC VNG ECLCSP GWGGLNCELA RVQCPDQCSG HGTYLPDSGL CSCDPNWMGP DCSVEVCSVD CGTHGVCIGG ACRCEEGWTG AACD QRVCH PRCIEHGTCK DGKCECREGW NGEHCTIGRQ TAGTETDGCP DLCNGNGRCT LGQNSWQCVC QTGWRGPGCN VAMET SCAD NKDNEGDGLV DCLDPDCCLQ SACQNSLLCR GSRDPLDIIQ QGQTDWPAVK SFYDRIKLLA GKDSTHIIPG DNPFNS SLV SLIRGQVVTM DGTPLVGVNV SFVKYPKYGY TITRQDGTFD LIANGGSALT LHFERAPFMS QERTVWLPWN SFYAMDT LV MKTEENSIPS CDLSGFVRPD PIIISSPLST FFSASPASNP IVPETQVLHE EIELPGTNVK LRYLSSRTAG YKSLLKIT M TQSTVPLNLI RVHLMVAVEG HLFQKSFQAS PNLAYTFIWD KTDAYGQRVY GLSDAVVSVG FEYETCPSLI LWEKRTALL QGFELDPSNL GGWSLDKHHT LNVKSGILHK GTGENQFLTQ QPAIITSIMG NGRRRSISCP SCNGLAEGNK LLAPVALAVG IDGSLFVGD FNYIRRIFPS RNVTSILELS NSPGHKYYLA VDPVTGSLYV SDTNSRRIYR VKSLSGAKDL AGNSEVVAGT G EQCLPFDE ARCGDGGKAV DATLMSPRGI AVDKNGLMYF VDATMIRKVD QNGIISTLLG SNDLTAVRPL SCDSSMDVAQ VR LEWPTDL AVNPMDNSLY VLENNVILRI TENHQVSIIA GRPMHCQVPG IDYSLSKLAI HSALESASAI AISHTGVLYI TET DEKKIN RLRQVTTNGE ICLLAGAASD CDCKNDVNCI CYSGDDAYAT DAILNSPSSL AVAPDGTIYI ADLGNIRIRA VSKN KPVLN AFNQYEAASP GEQELYVFNA DGIHQYTVSL VTGEYLYNFT YSADNDVTEL IDNNGNSLKI RRDSSGMPRH LLMPD NQII TLTVGTNGGL KAVSTQNLEL GLMTYDGNTG LLATKSDETG WTTFYDYDHE GRLTNVTRPT GVVTSLHREM EKSITI DIE NSNRDDDVTV ITNLSSVEAS YTVVQDQVRN SYQLCNNGTL RVMYANGMAV SFHSEPHVLA GTITPTIGRC NISLPME NG LNSIEWRLRK EQIKGKVTIF GRKLRVHGRN LLSIDYDRNI RTEKIYDDHR KFTLRIIYDQ VGRPFLWLPS SGLAAVNV S YFFNGRLAGL QRGAMSERTD IDKQGRIVSR MFADGKVWSY SYLDKSMVLL LQSQRQYIFE YDSSDRLHAV TMPSVARHS MSTHTSIGYI RNIYNPPESN ASVIFDYSDD GRILKTSFLG TGRQVFYKYG KLSKLSEIVY DSTAVTFGYD ETTGVLKMVN LQSGGFSCT IRYRKVGPLV DKQIYRFSEE GMINARFDYT YHDNSFRIAS IKPVISETPL PVDLYRYDEI SGKVEHFGKF G VIYYDINQ IITTAVMTLS KHFDTHGRIK EVQYEMFRSL MYWMTVQYDS MGRVIKRELK LGPYANTTKY TYDYDGDGQL QS VAVNDRP TWRYSYDLNG NLHLLNPGNS ARLMPLRYDL RDRITRLGDV QYKIDDDGYL CQRGSDIFEY NSKGLLTRAY NKA SGWSVQ YRYDGVGRRA SYKTNLGHHL QYFYSDLHNP TRITHVYNHS NSEITSLYYD LQGHLFAMES SSGEEYYVAS DNTG TPLAV FSINGLMIKQ LQYTAYGEIY YDSNPDFQMV IGFHGGLYDP LTKLVHFTQR DYDVLAGRWT SPDYTMWRNV GKEPA PFNL YMFKNNNPLS NELDLKNYVT DVKSWLVMFG FQLSNIIPGF PRAKMYFVPP PYELSESQAS ENGQLITGVQ QTTERH NQA FLALEGQVIT KKLHASIREK AGHWFATTTP IIGKGIMFAI KEGRVTTGVS SIASEDSRKV ASVLNNAYYL DKMHYSI EG KDTHYFVKIG AADGDLVTLG TTIGRKVLES GVNVTVSQPT LLVNGRTRRF TNIEFQYSTL LLSIRYGLTP DTLDEEKA R VLDQARQRAL GTAWAKEQQK ARDGREGSRL WTEGEKQQLL STGRVQGYEG YYVLPVEQYP ELADSSSNIQ FLRQNEMGK RGT UniProtKB: Teneurin-2 |
-Macromolecule #5: 2-acetamido-2-deoxy-beta-D-glucopyranose
| Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 5 / Number of copies: 9 / Formula: NAG |
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| Molecular weight | Theoretical: 221.208 Da |
| Chemical component information | ![]() ChemComp-NAG: |
-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 | 0.27 mg/mL | |||||||||
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| Buffer | pH: 7.5 Component:
Details: 25 mM HEPES, 300 mM NaCl, pH 7.5 | |||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV | |||||||||
| Details | Sample was monodisperse |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 8975 / Average electron dose: 42.303 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 105000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: Other / Chain - Initial model type: in silico model / Details: SWISSMODEL |
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| Refinement | Space: REAL / Protocol: RIGID BODY FIT |
| Output model | ![]() PDB-9g2h: |
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About Yorodumi




Keywords
Authors
United Kingdom, 1 items
Citation













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












































Homo sapiens (human)
FIELD EMISSION GUN

