5k70: Difference between revisions

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'''Unreleased structure'''


The entry 5k70 is ON HOLD  until Paper Publication
==Sidekick-2 immunoglobulin domains 1-4 H18R/N22S mutant==
<StructureSection load='5k70' size='340' side='right' caption='[[5k70]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5k70]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K70 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K70 FirstGlance]. <br>
</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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5k6u|5k6u]], [[5k6v|5k6v]], [[5k6w|5k6w]], [[5k6x|5k6x]], [[5k6y|5k6y]], [[5k6z|5k6z]]</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=5k70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k70 OCA], [http://pdbe.org/5k70 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k70 RCSB], [http://www.ebi.ac.uk/pdbsum/5k70 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k70 ProSAT]</span></td></tr>
</table>
<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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5k70" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Goodman, K M]]
[[Category: Honig, B]]
[[Category: Mannepalli, S]]
[[Category: Shapiro, L]]
[[Category: Cell adhesion]]
[[Category: Immunoglobulin]]

Revision as of 16:52, 3 October 2016

Sidekick-2 immunoglobulin domains 1-4 H18R/N22S mutant

5k70, resolution 2.70Å

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