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{{STRUCTURE_3m45| PDB=3m45 | SCENE= }}
==Crystal structure of Ig1 domain of mouse SynCAM 2==
===Crystal structure of Ig1 domain of mouse SynCAM 2===
<StructureSection load='3m45' size='340' side='right' caption='[[3m45]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
{{ABSTRACT_PUBMED_20739279}}
== Structural highlights ==
<table><tr><td colspan='2'>[[3m45]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M45 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M45 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cadm2, Igsf4d, Necl3, SynCAM 2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m45 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m45 RCSB], [http://www.ebi.ac.uk/pdbsum/3m45 PDBsum]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m4/3m45_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Select adhesion molecules connect pre- and postsynaptic membranes and organize developing synapses. The regulation of these trans-synaptic interactions is an important neurobiological question. We have previously shown that the synaptic cell adhesion molecules SynCAM 1 and 2 engage in homo- and heterophilic interactions and bridge the synaptic cleft to induce presynaptic terminals. Here, we demonstrate that site-specific N-glycosylation impacts the structure and function of adhesive SynCAM interactions. Through crystallographic analysis of SynCAM 2, we identified within the adhesive interface of its Ig1 domain an N-glycan on residue N60. Structural modeling of the corresponding SynCAM 1 Ig1 domain indicates that its glycosylation sites N70/N104 flank the binding interface of this domain. Mass-spectrometric and mutational studies confirm and characterize the modification of these three sites. These site-specific N-glycans affect SynCAM adhesion, yet act in a differential manner. While glycosylation of SynCAM 2 at N60 reduces adhesion, N-glycans at N70/N104 of SynCAM 1 increase its interactions. The modification of SynCAM 1 with sialic acids contributes to the glycan-dependent strengthening of its binding. Functionally, N-glycosylation promotes the trans-synaptic interactions of SynCAM 1 and is required for synapse induction. These results demonstrate that N-glycosylation of SynCAM proteins differentially affects their binding interface and implicate post-translational modification as a mechanism to regulate trans-synaptic adhesion.


==Function==
N-glycosylation at the SynCAM immunoglobulin interface modulates synaptic adhesion.,Fogel AI, Li Y, Giza J, Wang Q, Lam TT, Modis Y, Biederer T J Biol Chem. 2010 Aug 25. PMID:20739279<ref>PMID:20739279</ref>
[[http://www.uniprot.org/uniprot/CADM2_MOUSE CADM2_MOUSE]] Adhesion molecule that engages in homo- and heterophilic interactions with the other nectin-like family members, leading to cell aggregation. Important for synapse organization, providing regulated trans-synaptic adhesion. Preferentially binds to oligodendrocytes (By similarity).  


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[3m45]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M45 OCA].
</div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:020739279</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Modis, Y.]]
[[Category: Modis, Y]]
[[Category: Yue, L.]]
[[Category: Yue, L]]
[[Category: Cell adhesion]]
[[Category: Cell adhesion]]
[[Category: Dimer]]
[[Category: Dimer]]
Retrieved from "https://proteopedia.org/3m45"