Source:http://linkedlifedata.com/resource/pubmed/id/11856755
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
2002-4-29
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pubmed:abstractText |
Cadherin is a cell adhesion molecule crucial for epithelial and endothelial cell monolayer integrity. The previously solved x-ray crystallographic structure of the E-CAD12 cis-dimer displayed an unpaired Cys(9), which protruded away from the Cys(9) on the other protomer. To investigate the possible biological function of Cys(9) within the first repeat (the E-cadherin-derived N-terminal repeat), E-CAD1 was overexpressed and secreted into the periplasmic space of Escherichia coli cells. Recombinant E-CAD1 produced a mixed monomer and dimer in an equilibrium fashion. The dimer was linked by a disulfide through Cys(9) pairing. Analysis by high pressure liquid chromatography and electron microscopy suggested the existence of oligomeric complexes. Mutation at Trp(2) appears to indicate that these oligomeric complexes trans-dimerize. Interestingly, mutation of Cys(9) affected not only the cis-dimerization, but also the trans-oligomerization of E-CAD1. Accordingly, it is plausible that, under oxidative stress, the homophilic interactions of E-cadherin through E-CAD1 may be promoted and stabilized by this disulfide bond.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16002-10
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pubmed:dateRevised |
2010-12-3
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pubmed:meshHeading |
pubmed-meshheading:11856755-Amino Acid Sequence,
pubmed-meshheading:11856755-Cadherins,
pubmed-meshheading:11856755-Chromatography, High Pressure Liquid,
pubmed-meshheading:11856755-Cloning, Molecular,
pubmed-meshheading:11856755-Dimerization,
pubmed-meshheading:11856755-Disulfides,
pubmed-meshheading:11856755-Humans,
pubmed-meshheading:11856755-Models, Molecular,
pubmed-meshheading:11856755-Peptide Fragments,
pubmed-meshheading:11856755-Protein Conformation,
pubmed-meshheading:11856755-Recombinant Fusion Proteins,
pubmed-meshheading:11856755-Recombinant Proteins,
pubmed-meshheading:11856755-Transfection
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pubmed:year |
2002
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pubmed:articleTitle |
Disulfide bond formation promotes the cis- and trans-dimerization of the E-cadherin-derived first repeat.
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pubmed:affiliation |
Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, Kansas 66047, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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