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5k6y

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==Sidekick-2 immunoglobulin domains 1-4, crystal form 2==
==Sidekick-2 immunoglobulin domains 1-4, crystal form 2==
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<StructureSection load='5k6y' size='340' side='right' caption='[[5k6y]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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<StructureSection load='5k6y' size='340' side='right'caption='[[5k6y]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5k6y]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K6Y FirstGlance]. <br>
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<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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5k6u|5k6u]], [[5k6v|5k6v]], [[5k6w|5k6w]], [[5k6x|5k6x]], [[5k6z|5k6z]], [[5k70|5k70]]</td></tr>
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<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>
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<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=5k6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k6y OCA], [http://pdbe.org/5k6y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k6y RCSB], [http://www.ebi.ac.uk/pdbsum/5k6y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k6y ProSAT]</span></td></tr>
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<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>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/SDK2_MOUSE SDK2_MOUSE]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5k6y" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Goodman, K M]]
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[[Category: Large Structures]]
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[[Category: Honig, B]]
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[[Category: Mus musculus]]
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[[Category: Mannepalli, S]]
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[[Category: Goodman KM]]
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[[Category: Shapiro, L]]
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[[Category: Honig B]]
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[[Category: Cell adhesion]]
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[[Category: Mannepalli S]]
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[[Category: Immunoglobulin]]
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[[Category: Shapiro L]]

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Sidekick-2 immunoglobulin domains 1-4, crystal form 2

PDB ID 5k6y

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