Source:http://linkedlifedata.com/resource/pubmed/id/21269602
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2011-4-4
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| pubmed:databankReference | |
| pubmed:abstractText |
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-Å-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.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
1089-8638
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright © 2011 Elsevier Ltd. All rights reserved.
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| pubmed:issnType |
Electronic
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| pubmed:day |
22
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| pubmed:volume |
408
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
57-73
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| pubmed:dateRevised |
2011-10-24
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| pubmed:meshHeading |
pubmed-meshheading:21269602-Amino Acid Sequence,
pubmed-meshheading:21269602-Animals,
pubmed-meshheading:21269602-Antigens, CD,
pubmed-meshheading:21269602-Cadherins,
pubmed-meshheading:21269602-Cells, Cultured,
pubmed-meshheading:21269602-Chickens,
pubmed-meshheading:21269602-Chromatography, Gel,
pubmed-meshheading:21269602-Crystallography, X-Ray,
pubmed-meshheading:21269602-Endothelium, Vascular,
pubmed-meshheading:21269602-Glycosylation,
pubmed-meshheading:21269602-Humans,
pubmed-meshheading:21269602-Mice,
pubmed-meshheading:21269602-Microscopy, Atomic Force,
pubmed-meshheading:21269602-Molecular Sequence Data,
pubmed-meshheading:21269602-Protein Binding,
pubmed-meshheading:21269602-Protein Conformation,
pubmed-meshheading:21269602-Protein Multimerization,
pubmed-meshheading:21269602-Sequence Homology, Amino Acid
|
| pubmed:year |
2011
|
| pubmed:articleTitle |
Structure and binding mechanism of vascular endothelial cadherin: a divergent classical cadherin.
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| pubmed:affiliation |
Department of Biochemistry and Molecular Biophysics, Columbia University, 701 West 168th Street, New York, NY 10032, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|