5ftu: Difference between revisions
New page: '''Unreleased structure''' The entry 5ftu is ON HOLD Authors: Jackson, V.A., Mehmood, S., Chavent, M., Roversi, P., Carrasquero, M., del Toro, D., Seyit-Bremer, G., Ranaivoson, F.M., Co... |
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==Tetrameric complex of Latrophilin 3, Unc5D and FLRT2== | |||
<StructureSection load='5ftu' size='340' side='right'caption='[[5ftu]], [[Resolution|resolution]] 6.01Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ftu]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FTU FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 6.01Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=5ftu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ftu OCA], [https://pdbe.org/5ftu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ftu RCSB], [https://www.ebi.ac.uk/pdbsum/5ftu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ftu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/UNC5D_RAT UNC5D_RAT] Receptor for the netrin NTN4 that promotes neuronal cell survival. Plays a role in cell-cell adhesion and cell guidance. Receptor for netrin involved in cell migration. Plays a role in axon guidance by mediating axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding. May play a role in apoptosis in response to DNA damage. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (By similarity). Mediates cell-cell adhesion via its interaction with FLRT3 on an adjacent cell (By similarity).[UniProtKB:Q6UXZ4][UniProtKB:Q8K1S2] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Latrophilin adhesion-GPCRs (Lphn1-3 or ADGRL1-3) and Unc5 cell guidance receptors (Unc5A-D) interact with FLRT proteins (FLRT1-3), thereby promoting cell adhesion and repulsion, respectively. How the three proteins interact and function simultaneously is poorly understood. We show that Unc5D interacts with FLRT2 in cis, controlling cell adhesion in response to externally presented Lphn3. The ectodomains of the three proteins bind cooperatively. Crystal structures of the ternary complex formed by the extracellular domains reveal that Lphn3 dimerizes when bound to FLRT2:Unc5, resulting in a stoichiometry of 1:1:2 (FLRT2:Unc5D:Lphn3). This 1:1:2 complex further dimerizes to form a larger 'super-complex' (2:2:4), using a previously undescribed binding motif in the Unc5D TSP1 domain. Molecular dynamics simulations, point-directed mutagenesis and mass spectrometry demonstrate the stability and molecular properties of these complexes. Our data exemplify how receptors increase their functional repertoire by forming different context-dependent higher-order complexes. | |||
Super-complexes of adhesion GPCRs and neural guidance receptors.,Jackson VA, Mehmood S, Chavent M, Roversi P, Carrasquero M, Del Toro D, Seyit-Bremer G, Ranaivoson FM, Comoletti D, Sansom MS, Robinson CV, Klein R, Seiradake E Nat Commun. 2016 Apr 19;7:11184. doi: 10.1038/ncomms11184. PMID:27091502<ref>PMID:27091502</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5ftu" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Chavent | ==See Also== | ||
[[Category: Comoletti | *[[Latrophilin|Latrophilin]] | ||
[[Category: | *[[Netrin receptor|Netrin receptor]] | ||
[[Category: | == References == | ||
[[Category: Mehmood | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Sansom | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: Carrasquero M]] | ||
[[Category: Chavent M]] | |||
[[Category: Comoletti D]] | |||
[[Category: Jackson VA]] | |||
[[Category: Klein R]] | |||
[[Category: Mehmood S]] | |||
[[Category: Ranaivoson FM]] | |||
[[Category: Robinson CV]] | |||
[[Category: Roversi P]] | |||
[[Category: Sansom MSP]] | |||
[[Category: Seiradake E]] | |||
[[Category: Seyit-Bremer G]] | |||
[[Category: Del Toro D]] | |||
Latest revision as of 16:25, 26 July 2023
Tetrameric complex of Latrophilin 3, Unc5D and FLRT2Tetrameric complex of Latrophilin 3, Unc5D and FLRT2
Structural highlights
FunctionUNC5D_RAT Receptor for the netrin NTN4 that promotes neuronal cell survival. Plays a role in cell-cell adhesion and cell guidance. Receptor for netrin involved in cell migration. Plays a role in axon guidance by mediating axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding. May play a role in apoptosis in response to DNA damage. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (By similarity). Mediates cell-cell adhesion via its interaction with FLRT3 on an adjacent cell (By similarity).[UniProtKB:Q6UXZ4][UniProtKB:Q8K1S2] Publication Abstract from PubMedLatrophilin adhesion-GPCRs (Lphn1-3 or ADGRL1-3) and Unc5 cell guidance receptors (Unc5A-D) interact with FLRT proteins (FLRT1-3), thereby promoting cell adhesion and repulsion, respectively. How the three proteins interact and function simultaneously is poorly understood. We show that Unc5D interacts with FLRT2 in cis, controlling cell adhesion in response to externally presented Lphn3. The ectodomains of the three proteins bind cooperatively. Crystal structures of the ternary complex formed by the extracellular domains reveal that Lphn3 dimerizes when bound to FLRT2:Unc5, resulting in a stoichiometry of 1:1:2 (FLRT2:Unc5D:Lphn3). This 1:1:2 complex further dimerizes to form a larger 'super-complex' (2:2:4), using a previously undescribed binding motif in the Unc5D TSP1 domain. Molecular dynamics simulations, point-directed mutagenesis and mass spectrometry demonstrate the stability and molecular properties of these complexes. Our data exemplify how receptors increase their functional repertoire by forming different context-dependent higher-order complexes. Super-complexes of adhesion GPCRs and neural guidance receptors.,Jackson VA, Mehmood S, Chavent M, Roversi P, Carrasquero M, Del Toro D, Seyit-Bremer G, Ranaivoson FM, Comoletti D, Sansom MS, Robinson CV, Klein R, Seiradake E Nat Commun. 2016 Apr 19;7:11184. doi: 10.1038/ncomms11184. PMID:27091502[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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