View source for 3zyo


==Crystal structure of the N-terminal leucine rich repeats and immunoglobulin domain of netrin-G ligand-3==
<StructureSection load='3zyo' size='340' side='right'caption='[[3zyo]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zyo]] is a 1 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=3ZYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZYO 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]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3zyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zyo OCA], [https://pdbe.org/3zyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zyo RCSB], [https://www.ebi.ac.uk/pdbsum/3zyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zyo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LRC4B_MOUSE LRC4B_MOUSE] Synaptic adhesion protein. Regulates the formation of excitatory synapses. The trans-synaptic adhesion between LRRC4B and PTPRF regulates the formation of excitatory synapses in a bidirectional manner (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Brain wiring depends on cells making highly localized and selective connections through surface protein-protein interactions, including those between NetrinGs and NetrinG ligands (NGLs). The NetrinGs are members of the structurally uncharacterized netrin family. We present a comprehensive crystallographic analysis comprising NetrinG1-NGL1 and NetrinG2-NGL2 complexes, unliganded NetrinG2 and NGL3. Cognate NetrinG-NGL interactions depend on three specificity-conferring NetrinG loops, clasped tightly by matching NGL surfaces. We engineered these NGL surfaces to implant custom-made affinities for NetrinG1 and NetrinG2. In a cellular patterning assay, we demonstrate that NetrinG-binding selectivity can direct the sorting of a mixed population of NGLs into discrete cell surface subdomains. These results provide a molecular model for selectivity-based patterning in a neuronal recognition system, dysregulation of which is associated with severe neuropsychological disorders.

Structural basis for cell surface patterning through NetrinG-NGL interactions.,Seiradake E, Coles CH, Perestenko PV, Harlos K, McIlhinney RA, Aricescu AR, Jones EY EMBO J. 2011 Sep 23. doi: 10.1038/emboj.2011.346. PMID:21946559<ref>PMID:21946559</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zyo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Aricescu AR]]
[[Category: Coles CH]]
[[Category: Harlos K]]
[[Category: Jones EY]]
[[Category: McIlhinney RAJ]]
[[Category: Perestenko PV]]
[[Category: Seiradake E]]