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| | ==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]] 2.21Å' scene=''> | + | <StructureSection load='3m45' size='340' side='right'caption='[[3m45]], [[Resolution|resolution]] 2.21Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3m45]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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> | + | <table><tr><td colspan='2'>[[3m45]] is a 4 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=3M45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21Å</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 LK3 transgenic mice])</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'>[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://pdbe.org/3m45 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m45 RCSB], [http://www.ebi.ac.uk/pdbsum/3m45 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m45 ProSAT]</span></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=3m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m45 OCA], [https://pdbe.org/3m45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m45 RCSB], [https://www.ebi.ac.uk/pdbsum/3m45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m45 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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). | + | [https://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). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Modis, Y]] | + | [[Category: Mus musculus]] |
| - | [[Category: Yue, L]] | + | [[Category: Modis Y]] |
| - | [[Category: Cell adhesion]] | + | [[Category: Yue L]] |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: Disulfide bond]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Ig fold]]
| + | |
| - | [[Category: Immunoglobulin domain]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Transmembrane]]
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| Structural highlights
Function
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).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fogel AI, Li Y, Giza J, Wang Q, Lam TT, Modis Y, Biederer T. N-glycosylation at the SynCAM immunoglobulin interface modulates synaptic adhesion. J Biol Chem. 2010 Aug 25. PMID:20739279 doi:10.1074/jbc.M110.120865
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