5k6y
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Sidekick-2 immunoglobulin domains 1-4, crystal form 2== | |
+ | <StructureSection load='5k6y' size='340' side='right'caption='[[5k6y]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5k6y]] 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=5K6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K6Y 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]] 3.2Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <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=5k6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k6y OCA], [https://pdbe.org/5k6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k6y RCSB], [https://www.ebi.ac.uk/pdbsum/5k6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k6y ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/SDK2_MOUSE SDK2_MOUSE] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Sidekick (Sdk) 1 and 2 are related immunoglobulin superfamily cell adhesion proteins required for appropriate synaptic connections between specific subtypes of retinal neurons. Sdks mediate cell-cell adhesion with homophilic specificity that underlies their neuronal targeting function. Here we report crystal structures of Sdk1 and Sdk2 ectodomain regions, revealing similar homodimers mediated by the four N-terminal immunoglobulin domains (Ig1-4), arranged in a horseshoe conformation. These Ig1-4 horseshoes interact in a novel back-to-back orientation in both homodimers through Ig1:Ig2, Ig1:Ig1 and Ig3:Ig4 interactions. Structure-guided mutagenesis results show that this canonical dimer is required for both Sdk-mediated cell aggregation (via trans interactions) and Sdk clustering in isolated cells (via cis interactions). Sdk1/Sdk2 recognition specificity is encoded across Ig1-4, with Ig1-2 conferring the majority of binding affinity and differential specificity. We suggest that competition between cis and trans interactions provides a novel mechanism to sharpen the specificity of cell-cell interactions. | ||
- | + | Molecular basis of sidekick-mediated cell-cell adhesion and specificity.,Goodman KM, Yamagata M, Jin X, Mannepalli S, Katsamba PS, Ahlsen G, Sergeeva AP, Honig B, Sanes JR, Shapiro L Elife. 2016 Sep 19;5. pii: e19058. doi: 10.7554/eLife.19058. PMID:27644106<ref>PMID:27644106</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 5k6y" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Mus musculus]] | ||
+ | [[Category: Goodman KM]] | ||
+ | [[Category: Honig B]] | ||
+ | [[Category: Mannepalli S]] | ||
+ | [[Category: Shapiro L]] |
Current revision
Sidekick-2 immunoglobulin domains 1-4, crystal form 2
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