4yeb
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Structural characterization of a synaptic adhesion complex== | |
+ | <StructureSection load='4yeb' size='340' side='right'caption='[[4yeb]], [[Resolution|resolution]] 3.19Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4yeb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YEB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YEB 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]] 3.19Å</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=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=4yeb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yeb OCA], [https://pdbe.org/4yeb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yeb RCSB], [https://www.ebi.ac.uk/pdbsum/4yeb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yeb ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/AGRL3_MOUSE AGRL3_MOUSE] 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:22405201, PubMed:25728924, PubMed:26235031). Plays a role in the development of glutamatergic synapses in the cortex (PubMed:22405201, PubMed:24739570). Important in determining the connectivity rates between the principal neurons in the cortex (PubMed:24739570).<ref>PMID:22405201</ref> <ref>PMID:24739570</ref> <ref>PMID:25728924</ref> <ref>PMID:26235031</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Latrophilins (LPHNs) are adhesion-like G-protein-coupled receptors implicated in attention-deficit/hyperactivity disorder. Recently, LPHN3 was found to regulate excitatory synapse number through trans interactions with fibronectin leucine-rich repeat transmembrane 3 (FLRT3). By isothermal titration calorimetry, we determined that only the olfactomedin (OLF) domain of LPHN3 is necessary for FLRT3 association. By multi-crystal native single-wavelength anomalous diffraction phasing, we determined the crystal structure of the OLF domain. This structure is a five-bladed beta propeller with a Ca2+ ion bound in the central pore, which is capped by a mobile loop that allows the ion to exchange with the solvent. The crystal structure of the OLF/FLRT3 complex shows that LPHN3-OLF in the closed state binds with high affinity to the concave face of FLRT3-LRR with a combination of hydrophobic and charged residues. Our study provides structural and functional insights into the molecular mechanism underlying the contribution of LPHN3/FLRT3 to the development of glutamatergic synapses. | ||
- | + | Structural and Mechanistic Insights into the Latrophilin3-FLRT3 Complex that Mediates Glutamatergic Synapse Development.,Ranaivoson FM, Liu Q, Martini F, Bergami F, von Daake S, Li S, Lee D, Demeler B, Hendrickson WA, Comoletti D Structure. 2015 Jul 28. pii: S0969-2126(15)00275-0. doi:, 10.1016/j.str.2015.06.022. PMID:26235031<ref>PMID:26235031</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 4yeb" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | |
- | [[Category: | + | ==See Also== |
- | [[Category: Demeler | + | *[[Latrophilin|Latrophilin]] |
- | [[Category: | + | == References == |
- | [[Category: | + | <references/> |
- | [[Category: | + | __TOC__ |
- | [[Category: Liu | + | </StructureSection> |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Ranaivoson | + | [[Category: Mus musculus]] |
+ | [[Category: Bergami F]] | ||
+ | [[Category: Comoletti D]] | ||
+ | [[Category: Demeler B]] | ||
+ | [[Category: Hendrickson WA]] | ||
+ | [[Category: Lee D]] | ||
+ | [[Category: Li S]] | ||
+ | [[Category: Liu Q]] | ||
+ | [[Category: Martini F]] | ||
+ | [[Category: Ranaivoson FM]] | ||
+ | [[Category: Von Daake S]] |
Current revision
Structural characterization of a synaptic adhesion complex
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Categories: Large Structures | Mus musculus | Bergami F | Comoletti D | Demeler B | Hendrickson WA | Lee D | Li S | Liu Q | Martini F | Ranaivoson FM | Von Daake S