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3ppe
From Proteopedia
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| - | [[ | + | ==Crystal structure of chicken VE-cadherin EC1-2== |
| + | <StructureSection load='3ppe' size='340' side='right' caption='[[3ppe]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ppe]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PPE FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ppe RCSB], [http://www.ebi.ac.uk/pdbsum/3ppe PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Cadherin|Cadherin]] | *[[Cadherin|Cadherin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
| - | [[Category: Ahlsen, G | + | [[Category: Ahlsen, G]] |
| - | [[Category: Brasch, J | + | [[Category: Brasch, J]] |
| - | [[Category: Carnally, S M | + | [[Category: Carnally, S M]] |
| - | [[Category: Harrison, O J | + | [[Category: Harrison, O J]] |
| - | [[Category: Henderson, R M | + | [[Category: Henderson, R M]] |
| - | [[Category: Honig, B | + | [[Category: Honig, B]] |
| - | [[Category: Shapiro, L S | + | [[Category: Shapiro, L S]] |
[[Category: Beta barrel]] | [[Category: Beta barrel]] | ||
[[Category: Calcium dependent cell-cell adhesion]] | [[Category: Calcium dependent cell-cell adhesion]] | ||
Revision as of 10:58, 9 December 2014
Crystal structure of chicken VE-cadherin EC1-2
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