View source for 4bqc


==Crystal structure of the FN5 and FN6 domains of NEO1 bound to SOS==
<StructureSection load='4bqc' size='340' side='right'caption='[[4bqc]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bqc]] 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=4BQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BQC 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]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GU4:2,3,4,6-TETRA-O-SULFONATO-ALPHA-D-GLUCOPYRANOSE'>GU4</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=YYJ:1,3,4,6-tetra-O-sulfo-beta-D-fructofuranose'>YYJ</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=4bqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bqc OCA], [https://pdbe.org/4bqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bqc RCSB], [https://www.ebi.ac.uk/pdbsum/4bqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bqc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NEO1_MOUSE NEO1_MOUSE] May be involved as a regulatory protein in the transition of undifferentiated proliferating cells to their differentiated state. May also function as a cell adhesion molecule in a broad spectrum of embryonic and adult tissues.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Repulsive guidance molecule family members (RGMs) control fundamental and diverse cellular processes including motility and adhesion, immune cell regulation and systemic iron metabolism. However, it is not known how RGMs initiate signaling through their common cell surface receptor, neogenin (NEO1). Here, we present crystal structures of the NEO1 RGM-binding region and its complex with human RGMB (also called Dragon). The RGMB structure reveals a novel protein fold, a functionally important autocatalytic cleavage mechanism and provides a framework to explain numerous disease-linked mutations in RGMs. In the complex, two RGMB ectodomains conformationally stabilize the juxtamembrane regions of two NEO1 receptors, in a pH-dependent manner. We demonstrate that all RGM-NEO1 complexes share this architecture, which therefore represents the core of multiple signaling pathways.

Structure of the Repulsive Guidance Molecule (RGM)-Neogenin Signaling Hub.,Bell CH, Healey E, van Erp S, Bishop B, Tang C, Gilbert RJ, Aricescu AR, Pasterkamp RJ, Siebold C Science. 2013 Jun 6. PMID:23744777<ref>PMID:23744777</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bqc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Aricescu AR]]
[[Category: Bell CH]]
[[Category: Bishop B]]
[[Category: Gilbert RJC]]
[[Category: Healey E]]
[[Category: Pasterkamp RJ]]
[[Category: Siebold C]]
[[Category: Tang C]]
[[Category: VanErp S]]