spacer STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA
Primary citation
Title Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA.
Authors Chen, L.search; Glover, J.N.search; Hogan, P.G.search; Rao, A.search; Harrison, S.C.search
Journal NATUREsearch vol:392, pag:42-48 (1998), Identifiers: PubMed ID (9510247)search DOI (10.1038/32100)
Abstract The nuclear factor of activated T cells (NFAT) and the AP-1 heterodimer, Fos-Jun, cooperatively bind a composite DNA site and synergistically activate the expression of many immune-response genes. A 2.7-A-resolution crystal structure of the DNA-binding domains of NFAT, Fos and Jun, in a quaternary complex with a DNA fragment containing the distal antigen-receptor response element from the interleukin-2 gene promoter, shows an extended interface between NFAT and AP-1, facilitated by the bending of Fos and DNA. The tight association of the three proteins on DNA creates a continuous groove for the recognition of 15 base pairs.
MeSH terms Amino Acid Sequencesearch, Animalssearch, Binding Sitessearch, Crystallographysearch, X-Raysearch, DNAsearch, DNA-Binding Proteinssearch, Gene Expression Regulationsearch, Humanssearch, Micesearch, Modelssearch, Molecularsearch, Molecular Sequence Datasearch, Mutationsearch, NFATC Transcription Factorssearch, Nuclear Proteinssearch, Protein Conformationsearch, Proto-Oncogene Proteins c-fossearch, Proto-Oncogene Proteins c-junsearch, Recombinant Proteinssearch, T-Lymphocytessearch, Transcription Factor AP-1search, Transcription Factorssearch, Transcriptionsearch, Geneticsearch
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