rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1-2
|
pubmed:dateCreated |
1996-6-6
|
pubmed:abstractText |
The armadillo domain is a repeating sequence motif of a variety of proteins with different functions. Here we describe the structure of a synthetic single armadillo repeat solved by two-dimensional nuclear magnetic resonance spectroscopy. Our results indicate alpha-helical secondary structural elements in half of the residues.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
25
|
pubmed:volume |
383
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
31-6
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:8612785-Adenomatous Polyposis Coli Protein,
pubmed-meshheading:8612785-Amino Acid Sequence,
pubmed-meshheading:8612785-Animals,
pubmed-meshheading:8612785-Armadillo Domain Proteins,
pubmed-meshheading:8612785-Circular Dichroism,
pubmed-meshheading:8612785-Cytoskeletal Proteins,
pubmed-meshheading:8612785-Drosophila,
pubmed-meshheading:8612785-Drosophila Proteins,
pubmed-meshheading:8612785-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8612785-Molecular Sequence Data,
pubmed-meshheading:8612785-Peptides,
pubmed-meshheading:8612785-Protein Structure, Secondary,
pubmed-meshheading:8612785-Proteins,
pubmed-meshheading:8612785-Sequence Homology, Amino Acid,
pubmed-meshheading:8612785-Trans-Activators,
pubmed-meshheading:8612785-Transcription Factors
|
pubmed:year |
1996
|
pubmed:articleTitle |
Secondary structure of an armadillo single repeat from the APC protein.
|
pubmed:affiliation |
Max-Planck-Institut für Molekulare Physiologie, Abteilung Strukturelle Biologie, Dortmund, Germany.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|