5a2f: Difference between revisions

← Older edit Newer edit →

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

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Two membrane distal IgSF domains of CD166==
+<StructureSection load='5a2f' size='340' side='right' caption='[[5a2f]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5a2f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A2F FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a2e|5a2e]]</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=5a2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a2f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a2f RCSB], [http://www.ebi.ac.uk/pdbsum/5a2f PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CD166_HUMAN CD166_HUMAN]] Cell adhesion molecule that binds to CD6. Involved in neurite extension by neurons via heterophilic and homophilic interactions. May play a role in the binding of T- and B-cells to activated leukocytes, as well as in interactions between cells of the nervous system.
+<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.
-The entry 5a2f is ON HOLD  until Paper Publication
+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>
-Authors: Chappell, P.E., Johnson, S., Lea, S.M., Brown, M.H.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Two membrane distal IgSF domains of CD166
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Brown, M H]]
+[[Category: Chappell, P E]]
 [[Category: Johnson, S]]
-[[Category: Lea, S.M]]
+[[Category: Lea, S M]]
-[[Category: Brown, M.H]]
+[[Category: Activated leukocyte cell adhesion protein]]
-[[Category: Chappell, P.E]]
+[[Category: Alcam]]
+[[Category: Cell adhesion]]
+[[Category: Human]]