5afb: Difference between revisions
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''' | ==Crystal structure of the Latrophilin3 Lectin and Olfactomedin Domains== | ||
<StructureSection load='5afb' size='340' side='right' caption='[[5afb]], [[Resolution|resolution]] 2.16Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5afb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AFB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5afb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5afb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5afb RCSB], [http://www.ebi.ac.uk/pdbsum/5afb PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/LPHN3_MOUSE LPHN3_MOUSE]] May be involved in the development of glutamatergic synapses in the cortex. Important in determining the connectivity rates between the principal neurons in the cortex.<ref>PMID:24739570</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Latrophilins, receptors for spider venom alpha-latrotoxin, are adhesion type G-protein-coupled receptors with emerging functions in synapse development. The N-terminal region binds the endogenous cell adhesion molecule FLRT, a major regulator of cortical and synapse development. We present crystallographic data for the mouse Latrophilin3 lectin and olfactomedin-like (Olf) domains, thereby revealing the Olf beta-propeller fold and conserved calcium-binding site. We locate the FLRT-Latrophilin binding surfaces by a combination of sequence conservation analysis, point mutagenesis, and surface plasmon resonance experiments. In stripe assays, we show that wild-type Latrophilin3 and its high-affinity interactor FLRT2, but not the binding-impaired mutants we generated, promote HeLa cell adhesion. In contrast, cortical neurons expressing endogenous FLRTs are repelled by wild-type Latrophilin3 and not by the binding-impaired mutant. Taken together, we present molecular level insights into Latrophilin structure, its FLRT-binding mechanism, and a role for Latrophilin and FLRT that goes beyond a simply adhesive interaction. | |||
Structural Basis of Latrophilin-FLRT Interaction.,Jackson VA, Del Toro D, Carrasquero M, Roversi P, Harlos K, Klein R, Seiradake E Structure. 2015 Feb 17. pii: S0969-2126(15)00037-4. doi:, 10.1016/j.str.2015.01.013. PMID:25728924<ref>PMID:25728924</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Carrasquero, M]] | [[Category: Carrasquero, M]] | ||
[[Category: Harlos, K]] | [[Category: Harlos, K]] | ||
[[Category: Jackson, V A]] | |||
[[Category: Klein, R]] | |||
[[Category: Roversi, P]] | [[Category: Roversi, P]] | ||
[[Category: Seiradake, E]] | |||
[[Category: Toro, D del]] | |||
[[Category: Adhesion]] | |||
[[Category: Beta propeller]] | |||
[[Category: Guidance]] | |||
[[Category: Lectin]] | |||
[[Category: Olfactomedin]] | |||
[[Category: Repulsion]] | |||
[[Category: Signaling protein]] | |||
