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| | <StructureSection load='6ska' size='340' side='right'caption='[[6ska]], [[Resolution|resolution]] 3.86Å' scene=''> | | <StructureSection load='6ska' size='340' side='right'caption='[[6ska]], [[Resolution|resolution]] 3.86Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ska]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SKA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SKA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ska]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SKA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.86Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ska FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ska OCA], [http://pdbe.org/6ska PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ska RCSB], [http://www.ebi.ac.uk/pdbsum/6ska PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ska ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ska FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ska OCA], [https://pdbe.org/6ska PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ska RCSB], [https://www.ebi.ac.uk/pdbsum/6ska PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ska ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TEN2_CHICK TEN2_CHICK]] Acts as a ligand of the ADGRL1 receptor (By similarity). Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Promotes the formation of filopodia and enlarged growth cone in neuronal cells. Induces homophilic cell-cell adhesion. May also mediates axon guidance and heterophilic cell-cell adhesion. May function as a cellular signal transducer.<ref>PMID:10588872</ref> <ref>PMID:12361962</ref> <ref>PMID:12783990</ref> Ten-2 intracellular domain: Induces gene transcription inhibition. [[http://www.uniprot.org/uniprot/AGRL1_MOUSE AGRL1_MOUSE]] Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization. Receptor probably implicated in the regulation of exocytosis (By similarity). | + | [https://www.uniprot.org/uniprot/TEN2_CHICK TEN2_CHICK] Acts as a ligand of the ADGRL1 receptor (By similarity). Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Promotes the formation of filopodia and enlarged growth cone in neuronal cells. Induces homophilic cell-cell adhesion. May also mediates axon guidance and heterophilic cell-cell adhesion. May function as a cellular signal transducer.<ref>PMID:10588872</ref> <ref>PMID:12361962</ref> <ref>PMID:12783990</ref> Ten-2 intracellular domain: Induces gene transcription inhibition. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6ska" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6ska" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Latrophilin|Latrophilin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Carrasquero, M A]] | + | [[Category: Mus musculus]] |
| - | [[Category: Chu, A]] | + | [[Category: Carrasquero MA]] |
| - | [[Category: Lowe, E]] | + | [[Category: Chu A]] |
| - | [[Category: Seiradake, E]] | + | [[Category: Lowe E]] |
| - | [[Category: Adhesion]] | + | [[Category: Seiradake E]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Lphn]]
| + | |
| - | [[Category: Neuron]]
| + | |
| - | [[Category: Odz]]
| + | |
| - | [[Category: Olfactomedin]]
| + | |
| - | [[Category: Repulsion]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Synapse]]
| + | |
| - | [[Category: Yd-repeat]]
| + | |
| Structural highlights
Function
TEN2_CHICK Acts as a ligand of the ADGRL1 receptor (By similarity). Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Promotes the formation of filopodia and enlarged growth cone in neuronal cells. Induces homophilic cell-cell adhesion. May also mediates axon guidance and heterophilic cell-cell adhesion. May function as a cellular signal transducer.[1] [2] [3] Ten-2 intracellular domain: Induces gene transcription inhibition.
Publication Abstract from PubMed
Teneurins are ancient metazoan cell adhesion receptors that control brain development and neuronal wiring in higher animals. The extracellular C terminus binds the adhesion GPCR Latrophilin, forming a trans-cellular complex with synaptogenic functions. However, Teneurins, Latrophilins, and FLRT proteins are also expressed during murine cortical cell migration at earlier developmental stages. Here, we present crystal structures of Teneurin-Latrophilin complexes that reveal how the lectin and olfactomedin domains of Latrophilin bind across a spiraling beta-barrel domain of Teneurin, the YD shell. We couple structure-based protein engineering to biophysical analysis, cell migration assays, and in utero electroporation experiments to probe the importance of the interaction in cortical neuron migration. We show that binding of Latrophilins to Teneurins and FLRTs directs the migration of neurons using a contact repulsion-dependent mechanism. The effect is observed with cell bodies and small neurites rather than their processes. The results exemplify how a structure-encoded synaptogenic protein complex is also used for repulsive cell guidance.
Structural Basis of Teneurin-Latrophilin Interaction in Repulsive Guidance of Migrating Neurons.,Del Toro D, Carrasquero-Ordaz MA, Chu A, Ruff T, Shahin M, Jackson VA, Chavent M, Berbeira-Santana M, Seyit-Bremer G, Brignani S, Kaufmann R, Lowe E, Klein R, Seiradake E Cell. 2020 Jan 23;180(2):323-339.e19. doi: 10.1016/j.cell.2019.12.014. Epub 2020 , Jan 9. PMID:31928845[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rubin BP, Tucker RP, Martin D, Chiquet-Ehrismann R. Teneurins: a novel family of neuronal cell surface proteins in vertebrates, homologous to the Drosophila pair-rule gene product Ten-m. Dev Biol. 1999 Dec 1;216(1):195-209. PMID:10588872 doi:http://dx.doi.org/10.1006/dbio.1999.9503
- ↑ Rubin BP, Tucker RP, Brown-Luedi M, Martin D, Chiquet-Ehrismann R. Teneurin 2 is expressed by the neurons of the thalamofugal visual system in situ and promotes homophilic cell-cell adhesion in vitro. Development. 2002 Oct;129(20):4697-705. PMID:12361962
- ↑ Bagutti C, Forro G, Ferralli J, Rubin B, Chiquet-Ehrismann R. The intracellular domain of teneurin-2 has a nuclear function and represses zic-1-mediated transcription. J Cell Sci. 2003 Jul 15;116(Pt 14):2957-66. doi: 10.1242/jcs.00603. Epub 2003 Jun, 3. PMID:12783990 doi:http://dx.doi.org/10.1242/jcs.00603
- ↑ Del Toro D, Carrasquero-Ordaz MA, Chu A, Ruff T, Shahin M, Jackson VA, Chavent M, Berbeira-Santana M, Seyit-Bremer G, Brignani S, Kaufmann R, Lowe E, Klein R, Seiradake E. Structural Basis of Teneurin-Latrophilin Interaction in Repulsive Guidance of Migrating Neurons. Cell. 2020 Jan 23;180(2):323-339.e19. doi: 10.1016/j.cell.2019.12.014. Epub 2020 , Jan 9. PMID:31928845 doi:http://dx.doi.org/10.1016/j.cell.2019.12.014
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