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== | ==Human Teneurin-2 and human Latrophilin-3 binary complex== | ||
<StructureSection load='6vhh' size='340' side='right'caption='[[6vhh]]' scene=''> | <StructureSection load='6vhh' size='340' side='right'caption='[[6vhh]], [[Resolution|resolution]] 2.97Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VHH OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6vhh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VHH FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TENM2, KIAA1127, ODZ2, TNM2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ADGRL3, KIAA0768, LEC3, LPHN3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6vhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vhh OCA], [https://pdbe.org/6vhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vhh RCSB], [https://www.ebi.ac.uk/pdbsum/6vhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vhh ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/TEN2_HUMAN TEN2_HUMAN]] 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 (By similarity). May function as a cellular signal transducer.<ref>PMID:21724987</ref> Acts as a ligand of the ADGRL1 receptor. Mediates axon guidance and heterophilic cell-cell adhesion.<ref>PMID:21724987</ref> Induces gene transcription inhibition. [[https://www.uniprot.org/uniprot/AGRL3_HUMAN AGRL3_HUMAN]] Plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells (PubMed:26235030). Plays a role in the development of glutamatergic synapses in the cortex. Important in determining the connectivity rates between the principal neurons in the cortex.[UniProtKB:Q80TS3]<ref>PMID:26235030</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The trans-synaptic interaction of the cell-adhesion molecules teneurins (TENs) with latrophilins (LPHNs/ADGRLs) promotes excitatory synapse formation when LPHNs simultaneously interact with FLRTs. Insertion of a short alternatively-spliced region within TENs abolishes the TEN-LPHN interaction and switches TEN function to specify inhibitory synapses. How alternative-splicing regulates TEN-LPHN interaction remains unclear. Here, we report the 2.9 A resolution cryo-EM structure of the TEN2-LPHN3 complex, and describe the trimeric TEN2-LPHN3-FLRT3 complex. The structure reveals that the N-terminal lectin domain of LPHN3 binds to the TEN2 barrel at a site far away from the alternatively spliced region. Alternative-splicing regulates the TEN2-LPHN3 interaction by hindering access to the LPHN-binding surface rather than altering it. Strikingly, mutagenesis of the LPHN-binding surface of TEN2 abolishes the LPHN3 interaction and impairs excitatory but not inhibitory synapse formation. These results suggest that a multi-level coincident binding mechanism mediated by a cryptic adhesion complex between TENs and LPHNs regulates synapse specificity. | |||
Alternative splicing controls teneurin-latrophilin interaction and synapse specificity by a shape-shifting mechanism.,Li J, Xie Y, Cornelius S, Jiang X, Sando R, Kordon SP, Pan M, Leon K, Sudhof TC, Zhao M, Arac D Nat Commun. 2020 May 1;11(1):2140. doi: 10.1038/s41467-020-16029-7. PMID:32358586<ref>PMID:32358586</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6vhh" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Latrophilin|Latrophilin]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Arac, D]] | ||
[[Category: Li, J]] | |||
[[Category: Xie, Y]] | |||
[[Category: Zhao, M]] | |||
[[Category: Adhesion gpcr]] | |||
[[Category: Lphn]] | |||
[[Category: Membrane protein]] | |||
[[Category: Synapse]] | |||
[[Category: Teneurin]] | |||
Revision as of 15:20, 8 June 2021
Human Teneurin-2 and human Latrophilin-3 binary complex
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