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- EMDB-51021: Mouse Teneurin2 dimer variant A0B1 -

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Basic information

Entry
Database: EMDB / ID: EMD-51021
TitleMouse Teneurin2 dimer variant A0B1
Map dataSharpened map
Sample
  • Complex: Dimeric complex of mouse Teneurin2 A0B1 variant
    • Protein or peptide: Teneurin transmembrane protein 2
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
Keywordscell adhesion molecule / complex / homodimer / CELL ADHESION
Function / homology
Function and homology information


filopodium / 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
Teneurin intracellular, N-terminal / : / : / : / : / Teneurin Intracellular Region / Teneurin-3-like, galactose-binding domain-like / Teneurin antibiotic-binding-like domain / Teneurin 1-4, FN-plug domain / Teneurin TTR-like domain ...Teneurin intracellular, N-terminal / : / : / : / : / Teneurin Intracellular Region / Teneurin-3-like, galactose-binding domain-like / Teneurin antibiotic-binding-like domain / Teneurin 1-4, FN-plug domain / Teneurin TTR-like domain / Teneurin NHL domain / Teneurin N-terminal domain profile. / Tox-GHH domain / GHH signature containing HNH/Endo VII superfamily nuclease toxin / : / : / Teneurin YD-shell / Teneurin EGF domain / YD repeat / Rhs repeat-associated core / Carboxypeptidase-like, regulatory domain superfamily / Six-bladed beta-propeller, TolB-like / Epidermal growth factor-like domain. / EGF-like domain profile. / EGF-like domain signature 1. / EGF-like domain signature 2. / EGF-like domain
Similarity search - Domain/homology
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.48 Å
AuthorsBerbeira-Santana M / Zhou JC / el Omari K / Baker L / Seiradake E
Funding support United Kingdom, 1 items
OrganizationGrant numberCountry
Wellcome Trust226647/Z/22/Z United Kingdom
CitationJournal: Nat Commun / Year: 2026
Title: 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
DepositionJul 12, 2024-
Header (metadata) releaseJan 21, 2026-
Map releaseJan 21, 2026-
UpdateAug 12, 2026-
Current statusAug 12, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_51021.png

Downloads & links

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Map

FileDownload / File: emd_51021.map.gz / Format: CCP4 / Size: 163.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.94 Å/pix.
x 350 pix.
= 329. Å		0.94 Å/pix.
x 350 pix.
= 329. Å		0.94 Å/pix.
x 350 pix.
= 329. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.94 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.134
Minimum - Maximum-0.031162169 - 1.9253443
Average (Standard dev.)0.0016174912 (±0.027728163)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions350350350
Spacing350350350
CellA=B=C: 329.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: Raw map

Fileemd_51021_additional_1.map
AnnotationRaw map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map A

Fileemd_51021_half_map_1.map
AnnotationHalf map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map B

Fileemd_51021_half_map_2.map
AnnotationHalf map B
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 : Dimeric complex of mouse Teneurin2 A0B1 variant

EntireName: Dimeric complex of mouse Teneurin2 A0B1 variant
Components
  • Complex: Dimeric complex of mouse Teneurin2 A0B1 variant
    • Protein or peptide: Teneurin transmembrane protein 2
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose

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Supramolecule #1: Dimeric complex of mouse Teneurin2 A0B1 variant

SupramoleculeName: Dimeric complex of mouse Teneurin2 A0B1 variant / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Details: Dimeric complex purified by SEC after recombinant expression in HEK293T cells.
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 266.8826 KDa

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Macromolecule #1: Teneurin transmembrane protein 2

MacromoleculeName: Teneurin transmembrane protein 2 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 267.175906 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: 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 NGEHCTIDGC PDLCNGNGRC TLGQNSWQCV CQTGWRGPGC NVAMETSCAD NKDNE GDGL VDCLDPDCCL QSACQNSLLC RGSRDPLDII QQGQTDWPAV KSFYDRIKLL AGKDSTHIIP GDNPFNSSLV SLIRGQ VVT MDGTPLVGVN VSFVKYPKYG YTITRQDGTF DLIANGGSAL TLHFERAPFM SQERTVWLPW NSFYAMDTLV MKTEENS IP SCDLSGFVRP DPIIISSPLS TFFSASPASN PIVPETQVLH EEIELPGTNV KLRYLSSRTA GYKSLLKITM TQSTVPLN L IRVHLMVAVE GHLFQKSFQA SPNLAYTFIW DKTDAYGQRV YGLSDAVVSV GFEYETCPSL ILWEKRTALL QGFELDPSN LGGWSLDKHH TLNVKSGILH KGTGENQFLT QQPAIITSIM GNGRRRSISC PSCNGLAEGN KLLAPVALAV GIDGSLFVGD FNYIRRIFP SRNVTSILEL RNKEFKHSNS PGHKYYLAVD PVTGSLYVSD TNSRRIYRVK SLSGAKDLAG NSEVVAGTGE Q CLPFDEAR CGDGGKAVDA TLMSPRGIAV DKNGLMYFVD ATMIRKVDQN GIISTLLGSN DLTAVRPLSC DSSMDVAQVR LE WPTDLAV NPMDNSLYVL ENNVILRITE NHQVSIIAGR PMHCQVPGID YSLSKLAIHS ALESASAIAI SHTGVLYITE TDE KKINRL RQVTTNGEIC LLAGAASDCD CKNDVNCICY SGDDAYATDA ILNSPSSLAV APDGTIYIAD LGNIRIRAVS KNKP VLNAF NQYEAASPGE QELYVFNADG IHQYTVSLVT GEYLYNFTYS ADNDVTELID NNGNSLKIRR DSSGMPRHLL MPDNQ IITL TVGTNGGLKA VSTQNLELGL MTYDGNTGLL ATKSDETGWT TFYDYDHEGR LTNVTRPTGV VTSLHREMEK SITIDI ENS NRDDDVTVIT NLSSVEASYT VVQDQVRNSY QLCNNGTLRV MYANGMAVSF HSEPHVLAGT ITPTIGRCNI SLPMENG LN SIEWRLRKEQ IKGKVTIFGR KLRVHGRNLL SIDYDRNIRT EKIYDDHRKF TLRIIYDQVG RPFLWLPSSG LAAVNVSY F FNGRLAGLQR GAMSERTDID KQGRIVSRMF ADGKVWSYSY LDKSMVLLLQ SQRQYIFEYD SSDRLHAVTM PSVARHSMS THTSIGYIRN IYNPPESNAS VIFDYSDDGR ILKTSFLGTG RQVFYKYGKL SKLSEIVYDS TAVTFGYDET TGVLKMVNLQ SGGFSCTIR YRKVGPLVDK QIYRFSEEGM INARFDYTYH DNSFRIASIK PVISETPLPV DLYRYDEISG KVEHFGKFGV I YYDINQII TTAVMTLSKH FDTHGRIKEV QYEMFRSLMY WMTVQYDSMG RVIKRELKLG PYANTTKYTY DYDGDGQLQS VA VNDRPTW RYSYDLNGNL HLLNPGNSAR LMPLRYDLRD RITRLGDVQY KIDDDGYLCQ RGSDIFEYNS KGLLTRAYNK ASG WSVQYR YDGVGRRASY KTNLGHHLQY FYSDLHNPTR ITHVYNHSNS EITSLYYDLQ GHLFAMESSS GEEYYVASDN TGTP LAVFS INGLMIKQLQ YTAYGEIYYD SNPDFQMVIG FHGGLYDPLT KLVHFTQRDY DVLAGRWTSP DYTMWRNVGK EPAPF NLYM FKNNNPLSNE LDLKNYVTDV KSWLVMFGFQ LSNIIPGFPR AKMYFVPPPY ELSESQASEN GQLITGVQQT TERHNQ AFL ALEGQVITKK LHASIREKAG HWFATTTPII GKGIMFAIKE GRVTTGVSSI ASEDSRKVAS VLNNAYYLDK MHYSIEG KD THYFVKIGAA DGDLVTLGTT IGRKVLESGV NVTVSQPTLL VNGRTRRFTN IEFQYSTLLL SIRYGLTPDT LDEEKARV L DQARQRALGT AWAKEQQKAR DGREGSRLWT EGEKQQLLST GRVQGYEGYY VLPVEQYPEL ADSSSNIQFL RQNEMGKRG T

UniProtKB: Teneurin-2

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Macromolecule #5: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 5 / Number of copies: 9 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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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

Concentration0.35 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
300.0 mMNaClsodium chloride
25.0 mMHEPES

Details: 25 mM HEPES, 300 mM NaCl, pH 7.5
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 120 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.0001 kPa
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 294.15 K / Instrument: FEI VITROBOT MARK IV
DetailsSample was monodisperse

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Electron microscopy

MicroscopeFEI TALOS ARCTICA
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Number grids imaged: 1 / Number real images: 5212 / 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 / Cs: 2.7 mm / Nominal defocus max: 2.75 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 150000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 1037437
CTF correctionSoftware - Name: cryoSPARC / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.48 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 116348
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final 3D classificationNumber classes: 3 / Software - Name: cryoSPARC
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelChain - Source name: SwissModel / Chain - Initial model type: in silico model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-9g41:
Mouse Teneurin2 dimer variant A0B1

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