|Entry||Database: PDB / ID: 6cmx|
|Title||Human Teneurin 2 extra-cellular region|
|Keywords||MEMBRANE PROTEIN / Teneurin / Membrane protein / CNS|
|Function / homology||Teneurin Intracellular Region / EGF-like domain signature 2. / YD repeat / Carboxypeptidase-like, regulatory domain superfamily / GHH signature containing HNH/Endo VII superfamily nuclease toxin / Teneurin intracellular, N-terminal / EGF-like domain signature 1. / EGF-like calcium-binding domain / Quinoprotein amine dehydrogenase, beta chain-like / Six-bladed beta-propeller, TolB-like ...Teneurin Intracellular Region / EGF-like domain signature 2. / YD repeat / Carboxypeptidase-like, regulatory domain superfamily / GHH signature containing HNH/Endo VII superfamily nuclease toxin / Teneurin intracellular, N-terminal / EGF-like domain signature 1. / EGF-like calcium-binding domain / Quinoprotein amine dehydrogenase, beta chain-like / Six-bladed beta-propeller, TolB-like / EGF-like domain / EGF-like domain profile. / Tox-GHH domain / Teneurin N-terminal domain profile. / Rhs repeat-associated core / Teneurin-2/3 / EGF-like, conserved site / retrograde trans-synaptic signaling by trans-synaptic protein complex / positive regulation of filopodium assembly / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / neuron development / calcium-mediated signaling using intracellular calcium source / filopodium / cell adhesion molecule binding / cell-cell adhesion / PML body / postsynaptic membrane / cell-cell junction / axon guidance / growth cone / dendritic spine / cell junction / neuron projection / synapse / dendrite / signaling receptor binding / calcium ion binding / protein heterodimerization activity / endoplasmic reticulum / integral component of plasma membrane / Golgi apparatus / negative regulation of transcription by RNA polymerase II / signal transduction / protein homodimerization activity / plasma membrane / nucleus / Teneurin-2|
Function and homology information
|Specimen source||Homo sapiens (human)|
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / 3.1 Å resolution|
|Authors||Shalev-Benami, M. / Li, J. / Sudhof, T. / Skiniotis, G. / Arac, D.|
|Citation||Journal: Cell / Year: 2018|
Title: Structural Basis for Teneurin Function in Circuit-Wiring: A Toxin Motif at the Synapse.
Authors: Jingxian Li / Moran Shalev-Benami / Richard Sando / Xian Jiang / Amanuel Kibrom / Jie Wang / Katherine Leon / Christopher Katanski / Olha Nazarko / Yue C Lu / Thomas C Südhof / Georgios Skiniotis / Demet Araç
Abstract: Teneurins (TENs) are cell-surface adhesion proteins with critical roles in tissue development and axon guidance. Here, we report the 3.1-Å cryoelectron microscopy structure of the human TEN2 ...Teneurins (TENs) are cell-surface adhesion proteins with critical roles in tissue development and axon guidance. Here, we report the 3.1-Å cryoelectron microscopy structure of the human TEN2 extracellular region (ECR), revealing a striking similarity to bacterial Tc-toxins. The ECR includes a large β barrel that partially encapsulates a C-terminal domain, which emerges to the solvent through an opening in the mid-barrel region. An immunoglobulin (Ig)-like domain seals the bottom of the barrel while a β propeller is attached in a perpendicular orientation. We further show that an alternatively spliced region within the β propeller acts as a switch to regulate trans-cellular adhesion of TEN2 to latrophilin (LPHN), a transmembrane receptor known to mediate critical functions in the central nervous system. One splice variant activates trans-cellular signaling in a LPHN-dependent manner, whereas the other induces inhibitory postsynaptic differentiation. These results highlight the unusual structural organization of TENs giving rise to their multifarious functions.
SummaryFull reportAbout validation report
|Date||Deposition: Mar 6, 2018 / Release: Jul 25, 2018|
|Structure viewer||Molecule: |
Downloads & links
|#1: Protein/peptide|| |
Mass: 224005.812 Da / Num. of mol.: 1 / Source: (gene. exp.) Homo sapiens (human) / Gene: TENM2, KIAA1127, ODZ2, TNM2 / Production host: Trichoplusia ni (cabbage looper) / Strain (production host): High-Five / References: UniProt: Q9NT68*PLUS
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / Reconstruction method: single particle reconstruction|
|Component||Name: Teneurin 2 extra-cellular region / Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: 1 / Source: RECOMBINANT|
|Molecular weight||Value: 0.215 MDa / Experimental value: NO|
|Source (natural)||Organism: Homo sapiens (human)|
|Source (recombinant)||Organism: Trichoplusia ni (cabbage looper)|
|Buffer solution||pH: 8|
|Specimen||Conc.: 0.15 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Grid material: COPPER / Grid type: Quantifoil R2/2|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 298.15 kelvins|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Microscope model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Electron dose: 44 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|Software||Name: PHENIX / Version: 1.12_2829: / Classification: refinement|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|3D reconstruction||Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 426107 / Symmetry type: POINT|
|Refine LS restraints|
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