4v2c

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==mouse FLRT2 LRR domain in complex with rat Unc5D Ig1 domain==
==mouse FLRT2 LRR domain in complex with rat Unc5D Ig1 domain==
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<StructureSection load='4v2c' size='340' side='right' caption='[[4v2c]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
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<StructureSection load='4v2c' size='340' side='right'caption='[[4v2c]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4v2c]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V2C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V2C FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4v2c]] is a 4 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=4V2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V2C FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4v2a|4v2a]], [[4v2b|4v2b]], [[4v2d|4v2d]], [[4v2e|4v2e]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4&#8491;</td></tr>
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<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=4v2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v2c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v2c RCSB], [http://www.ebi.ac.uk/pdbsum/4v2c PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4v2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v2c OCA], [https://pdbe.org/4v2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v2c RCSB], [https://www.ebi.ac.uk/pdbsum/4v2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v2c ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FLRT2_MOUSE FLRT2_MOUSE] Functions in cell-cell adhesion, cell migration and axon guidance. Mediates cell-cell adhesion via its interactions with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells (PubMed:21350012, PubMed:25728924 PubMed:25374360). May play a role in the migration of cortical neurons during brain development via its interaction with UNC5D (PubMed:21673655). Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5D, and possibly also other UNC-5 family members (PubMed:21673655, PubMed:25728924). Plays a role in fibroblast growth factor-mediated signaling cascades (PubMed:16872596). Required for normal organization of the cardiac basement membrane during embryogenesis, and for normal embryonic epicardium and heart morphogenesis (PubMed:21350012).<ref>PMID:16872596</ref> <ref>PMID:21350012</ref> <ref>PMID:21673655</ref> <ref>PMID:25374360</ref> <ref>PMID:25728924</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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FLRTs are broadly expressed proteins with the unique property of acting as homophilic cell adhesion molecules and as heterophilic repulsive ligands of Unc5/Netrin receptors. How these functions direct cell behavior and the molecular mechanisms involved remain largely unclear. Here we use X-ray crystallography to reveal the distinct structural bases for FLRT-mediated cell adhesion and repulsion in neurons. We apply this knowledge to elucidate FLRT functions during cortical development. We show that FLRTs regulate both the radial migration of pyramidal neurons, as well as their tangential spread. Mechanistically, radial migration is controlled by repulsive FLRT2-Unc5D interactions, while spatial organization in the tangential axis involves adhesive FLRT-FLRT interactions. Further, we show that the fundamental mechanisms of FLRT adhesion and repulsion are conserved between neurons and vascular endothelial cells. Our results reveal FLRTs as powerful guidance factors with structurally encoded repulsive and adhesive surfaces.
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FLRT structure: balancing repulsion and cell adhesion in cortical and vascular development.,Seiradake E, del Toro D, Nagel D, Cop F, Hartl R, Ruff T, Seyit-Bremer G, Harlos K, Border EC, Acker-Palmer A, Jones EY, Klein R Neuron. 2014 Oct 22;84(2):370-85. doi: 10.1016/j.neuron.2014.10.008. Epub 2014, Oct 22. PMID:25374360<ref>PMID:25374360</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4v2c" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Netrin receptor|Netrin receptor]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acker-Palmer, A]]
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[[Category: Large Structures]]
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[[Category: Border, E C]]
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[[Category: Mus musculus]]
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[[Category: Cop, F]]
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[[Category: Rattus norvegicus]]
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[[Category: Haertl, R]]
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[[Category: Acker-Palmer A]]
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[[Category: Harlos, K]]
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[[Category: Border EC]]
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[[Category: Jones, E Y]]
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[[Category: Cop F]]
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[[Category: Klein, R]]
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[[Category: Haertl R]]
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[[Category: Nagel, D]]
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[[Category: Harlos K]]
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[[Category: Ruff, T]]
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[[Category: Jones EY]]
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[[Category: Seiradake, E]]
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[[Category: Klein R]]
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[[Category: Seyit-Bremer, G]]
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[[Category: Nagel D]]
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[[Category: Toro, D del]]
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[[Category: Ruff T]]
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[[Category: Apoptosis]]
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[[Category: Seiradake E]]
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[[Category: Leucine-rich repeat]]
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[[Category: Seyit-Bremer G]]
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[[Category: Unc5]]
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[[Category: Del Toro D]]
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[[Category: Uncoordinated-5]]
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Current revision

mouse FLRT2 LRR domain in complex with rat Unc5D Ig1 domain

PDB ID 4v2c

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