Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-6-19
pubmed:abstractText
The transcription of interferon (IFN) and IFN-inducible genes is mainly regulated by the interferon regulatory factor (IRF) family of proteins, which recognize a unique AAGTGA hexamer repeat motif in the regulatory region of IFN genes. A DNA-binding domain of approximately 100 amino acids has been commonly found in the IRF family of proteins, but it has no sequence homology to known DNA-binding motifs. Elucidation of the structures of members of the IRF family is therefore useful to the understanding of the regulation and evolution of the immune system at the structural level.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0969-2126
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
491-500
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9562558-Amino Acid Sequence, pubmed-meshheading:9562558-Animals, pubmed-meshheading:9562558-Bacterial Proteins, pubmed-meshheading:9562558-DNA, pubmed-meshheading:9562558-DNA-Binding Proteins, pubmed-meshheading:9562558-Evolution, Molecular, pubmed-meshheading:9562558-Helix-Turn-Helix Motifs, pubmed-meshheading:9562558-Interferon Regulatory Factor-2, pubmed-meshheading:9562558-Interferon-beta, pubmed-meshheading:9562558-Kluyveromyces, pubmed-meshheading:9562558-Magnetic Resonance Spectroscopy, pubmed-meshheading:9562558-Mice, pubmed-meshheading:9562558-Molecular Sequence Data, pubmed-meshheading:9562558-Nucleic Acid Conformation, pubmed-meshheading:9562558-Protein Structure, Secondary, pubmed-meshheading:9562558-Recombinant Proteins, pubmed-meshheading:9562558-Repressor Proteins, pubmed-meshheading:9562558-Sequence Alignment, pubmed-meshheading:9562558-Transcription Factors
pubmed:year
1998
pubmed:articleTitle
Solution structure of the IRF-2 DNA-binding domain: a novel subgroup of the winged helix-turn-helix family.
pubmed:affiliation
Institute for Protein Research, Osaka University, Suita, Osaka, 565, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't