View source for 3ppe


==Crystal structure of chicken VE-cadherin EC1-2==
<StructureSection load='3ppe' size='340' side='right'caption='[[3ppe]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ppe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PPE 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=3ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppe OCA], [https://pdbe.org/3ppe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ppe RCSB], [https://www.ebi.ac.uk/pdbsum/3ppe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CADH5_CHICK CADH5_CHICK] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. This cadherin may play a important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions.<ref>PMID:21269602</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Vascular endothelial cadherin (VE-cadherin), a divergent member of the type II classical cadherin family of cell adhesion proteins, mediates homophilic adhesion in the vascular endothelium. Previous investigations with a bacterially produced protein suggested that VE-cadherin forms cell surface trimers that bind between apposed cells to form hexamers. Here we report studies of mammalian-produced VE-cadherin ectodomains suggesting that, like other classical cadherins, VE-cadherin forms adhesive trans dimers between monomers located on opposing cell surfaces. Trimerization of the bacterially produced protein appears to be an artifact that arises from a lack of glycosylation. We also present the 2.1-A-resolution crystal structure of the VE-cadherin EC1-2 adhesive region, which reveals homodimerization via the strand-swap mechanism common to classical cadherins. In common with type II cadherins, strand-swap binding involves two tryptophan anchor residues, but the adhesive interface resembles type I cadherins in that VE-cadherin does not form a large nonswapped hydrophobic surface. Thus, VE-cadherin is an outlier among classical cadherins, with characteristics of both type I and type II subfamilies.

Structure and binding mechanism of vascular endothelial cadherin: a divergent classical cadherin.,Brasch J, Harrison OJ, Ahlsen G, Carnally SM, Henderson RM, Honig B, Shapiro L J Mol Biol. 2011 Apr 22;408(1):57-73. Epub 2011 Jan 24. PMID:21269602<ref>PMID:21269602</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ppe" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cadherin 3D structures|Cadherin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Ahlsen G]]
[[Category: Brasch J]]
[[Category: Carnally SM]]
[[Category: Harrison OJ]]
[[Category: Henderson RM]]
[[Category: Honig B]]
[[Category: Shapiro LS]]