View source for 4of0


==Crystal Structure of SYG-1 D1-D2, refolded==
<StructureSection load='4of0' size='340' side='right'caption='[[4of0]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4of0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OF0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4of0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4of0 OCA], [https://pdbe.org/4of0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4of0 RCSB], [https://www.ebi.ac.uk/pdbsum/4of0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4of0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYG1_CAEEL SYG1_CAEEL] Cell adhesion protein (PubMed:15035988). Involved in synapse formation in the HSNL egg-laying motor neuron (PubMed:12628183, PubMed:15035988, PubMed:21858180, PubMed:24485456). Inhibits assembly of the SCF(sel-10) E3 ubiquitin ligase complex at synapses, and protects them from elimination (PubMed:17626846). Also required for F-actin assembly at the synaptic region and for axon branch formation (PubMed:24439377).<ref>PMID:12628183</ref> <ref>PMID:15035988</ref> <ref>PMID:17626846</ref> <ref>PMID:21858180</ref> <ref>PMID:24439377</ref> <ref>PMID:24485456</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SYG-1 and SYG-2 are multipurpose cell adhesion molecules (CAMs) that have evolved across all major animal taxa to participate in diverse physiological functions, ranging from synapse formation to formation of the kidney filtration barrier. In the crystal structures of several SYG-1 and SYG-2 orthologs and their complexes, we find that SYG-1 orthologs homodimerize through a common, bispecific interface that similarly mediates an unusual orthogonal docking geometry in the heterophilic SYG-1/SYG-2 complex. C. elegans SYG-1's specification of proper synapse formation in vivo closely correlates with the heterophilic complex affinity, which appears to be tuned for optimal function. Furthermore, replacement of the interacting domains of SYG-1 and SYG-2 with those from CAM complexes that assume alternative docking geometries or the introduction of segmental flexibility compromised synaptic function. These results suggest that SYG extracellular complexes do not simply act as "molecular velcro" and that their distinct structural features are important in instructing synaptogenesis. PAPERFLICK:

Extracellular Architecture of the SYG-1/SYG-2 Adhesion Complex Instructs Synaptogenesis.,Ozkan E, Chia PH, Wang RR, Goriatcheva N, Borek D, Otwinowski Z, Walz T, Shen K, Garcia KC Cell. 2014 Jan 30;156(3):482-94. doi: 10.1016/j.cell.2014.01.004. PMID:24485456<ref>PMID:24485456</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4of0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Garcia KC]]
[[Category: Ozkan E]]