View source for 6fg9


==Mouse SORCS2 ectodomain (sortilin related VPS10 domain containing receptor 2)==
<StructureSection load='6fg9' size='340' side='right'caption='[[6fg9]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fg9]] 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=6FG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FG9 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]] 4.2&#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></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=6fg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fg9 OCA], [https://pdbe.org/6fg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fg9 RCSB], [https://www.ebi.ac.uk/pdbsum/6fg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fg9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SORC2_MOUSE SORC2_MOUSE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Signaling of SorCS receptors by proneurotrophin ligands regulates neuronal plasticity, induces apoptosis and is associated with mental disorders. The detailed structure of SorCS2 and its extracellular specificity are unresolved. Here we report crystal structures of the SorCS2-NGF complex and unliganded SorCS2 ectodomain, revealing cross-braced SorCS2 homodimers with two NGF dimers bound in a 2:4 stoichiometry. Five out of six SorCS2 domains directly contribute to dimer formation and a C-terminal membrane proximal unreported domain, with an RNA recognition motif fold, locks the dimer in an intermolecular head-to-tail interaction. The complex structure shows an altered SorCS2 conformation indicating substantial structural plasticity. Both NGF dimer chains interact exclusively with the top face of a SorCS2 beta-propeller. Biophysical experiments reveal that NGF, proNGF, and proBDNF bind at this site on SorCS2. Taken together, our data reveal a structurally flexible SorCS2 receptor that employs the large beta-propeller as a ligand binding platform.

Structural insights into SorCS2-Nerve Growth Factor complex formation.,Leloup N, Chataigner LMP, Janssen BJC Nat Commun. 2018 Jul 30;9(1):2979. doi: 10.1038/s41467-018-05405-z. PMID:30061605<ref>PMID:30061605</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6fg9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Janssen BJC]]
[[Category: Leloup NOL]]