Linked Life Data

9506523

Source:http://linkedlifedata.com/resource/pubmed/id/9506523

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1998-3-30
pubmed:abstractText
The nuclear factor of the activated T cell (NFAT) family of transcription factors regulates cytokine gene expression by binding to the promoter/enhancer regions of antigen-responsive genes, usually in cooperation with heterologous DNA-binding partners. Here we report the solution structure of the binary complex formed between the core DNA-binding domain of human NFATC1 and the ARRE2 DNA site from the interleukin-2 promoter. The structure reveals that DNA binding induces the folding of key structural elements that are required for both sequence-specific recognition and the establishment of cooperative protein-protein contacts. The orientation of the NFAT DNA-binding domain observed in the binary NFATC1-DBD*/ DNA complex is distinct from that seen in the ternary NFATC2/AP-1/DNA complex, suggesting that the domain reorients upon formation of a cooperative transcriptional complex.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
92
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
687-96
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:9506523-Amino Acid Sequence, pubmed-meshheading:9506523-DNA, pubmed-meshheading:9506523-DNA-Binding Proteins, pubmed-meshheading:9506523-Enhancer Elements, Genetic, pubmed-meshheading:9506523-Humans, pubmed-meshheading:9506523-Interleukin-2, pubmed-meshheading:9506523-Models, Molecular, pubmed-meshheading:9506523-Molecular Sequence Data, pubmed-meshheading:9506523-NFATC Transcription Factors, pubmed-meshheading:9506523-Nuclear Magnetic Resonance, Biomolecular, pubmed-meshheading:9506523-Nuclear Proteins, pubmed-meshheading:9506523-Nucleic Acid Conformation, pubmed-meshheading:9506523-Oligodeoxyribonucleotides, pubmed-meshheading:9506523-Point Mutation, pubmed-meshheading:9506523-Protein Conformation, pubmed-meshheading:9506523-Sequence Alignment, pubmed-meshheading:9506523-Transcription Factors
pubmed:year
1998
pubmed:articleTitle
Solution structure of the core NFATC1/DNA complex.
pubmed:affiliation
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't