3m45: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{STRUCTURE_3m45|  PDB=3m45  |  SCENE=  }}
-===Crystal structure of Ig1 domain of mouse SynCAM 2===
-{{ABSTRACT_PUBMED_20739279}}
-==Function==
+==Crystal structure of Ig1 domain of mouse SynCAM 2==
-[[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).
+<StructureSection load='3m45' size='340' side='right'caption='[[3m45]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21&#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=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>
+== Function ==
+[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 ==
+[[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/initialview03.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/main_output.php?pdb_ID=3m45 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.
-==About this Structure==
+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>
-[[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].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<ref group="xtra">PMID:020739279</ref><references group="xtra"/><references/>
+</div>
+<div class="pdbe-citations 3m45" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Modis, Y.]]
+[[Category: Modis Y]]
-[[Category: Yue, L.]]
+[[Category: Yue L]]
-[[Category: Cell adhesion]]
-[[Category: Dimer]]
-[[Category: Disulfide bond]]
-[[Category: Glycoprotein]]
-[[Category: Ig fold]]
-[[Category: Immunoglobulin domain]]
-[[Category: Membrane]]
-[[Category: Transmembrane]]