View source for 5a2e


==Extracellular SRCR domains of human CD6==
<StructureSection load='5a2e' size='340' side='right'caption='[[5a2e]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5a2e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A2E 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]] 3.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=5a2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a2e OCA], [https://pdbe.org/5a2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a2e RCSB], [https://www.ebi.ac.uk/pdbsum/5a2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a2e ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CD6_HUMAN CD6_HUMAN] Involved in cell adhesion. Binds to CD166.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CD6 is a transmembrane protein with an extracellular region containing three scavenger receptor cysteine rich (SRCR) domains. The membrane proximal domain of CD6 binds the N-terminal immunoglobulin superfamily (IgSF) domain of another cell surface receptor, CD166, which also engages in homophilic interactions. CD6 expression is mainly restricted to T cells, and the interaction between CD6 and CD166 regulates T-cell activation. We have solved the X-ray crystal structures of the three SRCR domains of CD6 and two N-terminal domains of CD166. This first structure of consecutive SRCR domains reveals a nonlinear organization. We characterized the binding sites on CD6 and CD166 and showed that a SNP in CD6 causes glycosylation that hinders the CD6/CD166 interaction. Native mass spectrometry analysis showed that there is competition between the heterophilic and homophilic interactions. These data give insight into how interactions of consecutive SRCR domains are perturbed by SNPs and potential therapeutic reagents.

Structures of CD6 and Its Ligand CD166 Give Insight into Their Interaction.,Chappell PE, Garner LI, Yan J, Metcalfe C, Hatherley D, Johnson S, Robinson CV, Lea SM, Brown MH Structure. 2015 Jun 22. pii: S0969-2126(15)00222-1. doi:, 10.1016/j.str.2015.05.019. PMID:26146185<ref>PMID:26146185</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5a2e" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Brown MH]]
[[Category: Chappell PE]]
[[Category: Johnson S]]
[[Category: Lea SM]]