Source:http://linkedlifedata.com/resource/pubmed/id/12074582
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2002-6-20
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pubmed:abstractText |
The solution structure of the EGF-like domain of betacellulin (BTCe), a newly discovered member of the epidermal growth factor (EGF) family, has been determined using two-dimensional nuclear magnetic resonance spectroscopy. This is the first report to identify the solution structure of the EGF-family ligand monomers that interact with both ErbB-1 and ErbB-4. The solution structure of BTCe was calculated using 538 NMR-derived restraints. The overall structure of BTCe was stabilized by three disulfide bonds, a hydrophobic core, and 23 hydrogen bonds. It appears that BTCe is comprised of five beta-strands and one short 3(10) helical turn. The secondary structural elements of BTCe are basically similar to those of the other EGF-family proteins, except that several significant variations of the structural properties were found. It is suggested that the structural variations between BTCe and the other EGF-family ligands may affect the specific receptor-recognition properties of EGF-family ligands.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Growth Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/betacellulin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
294
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1040-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12074582-Amino Acid Sequence,
pubmed-meshheading:12074582-Animals,
pubmed-meshheading:12074582-Epidermal Growth Factor,
pubmed-meshheading:12074582-Growth Substances,
pubmed-meshheading:12074582-Humans,
pubmed-meshheading:12074582-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:12074582-Ligands,
pubmed-meshheading:12074582-Mice,
pubmed-meshheading:12074582-Models, Molecular,
pubmed-meshheading:12074582-Molecular Sequence Data,
pubmed-meshheading:12074582-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:12074582-Protein Structure, Tertiary,
pubmed-meshheading:12074582-Static Electricity
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pubmed:year |
2002
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pubmed:articleTitle |
Solution structure of betacellulin, a new member of EGF-family ligands.
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pubmed:affiliation |
Bio-oriented Technology Research Advancement Institution, 1-40-2 Nisshin, Saitama, Saitama 331-8537, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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