1T2K

Structure Of The DNA Binding Domains Of IRF3, ATF-2 and Jun Bound To DNA

Summary for 1T2K

• Entry DOI: 10.2210/pdb1t2k/pdb
• Descriptor: 31-MER, Interferon regulatory factor 3, Transcription factor AP-1, ... (6 entities in total)
• Functional Keywords: protein dna complex, transcription, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q14653; Nucleus: P05412 P15336
• Total number of polymer chains: 6
• Total formula weight: 59625.96

Authors

Panne, D.,Maniatis, T.,Harrison, S.C. (deposition date: 2004-04-21, release date: 2004-11-16, Last modification date: 2023-08-23)

Primary citation

Panne, D.,Maniatis, T.,Harrison, S.C.
Crystal structure of ATF-2/c-Jun and IRF-3 bound to the interferon-beta enhancer.
Embo J., 23:4384-4393, 2004

PubMed Abstract: Transcriptional activation of the interferon-beta (IFN-beta) gene requires assembly of an enhanceosome containing the transcription factors ATF-2/c-Jun, IRF-3/IRF-7, NF-kappaB and HMGI(Y). These factors cooperatively bind a composite DNA site and activate expression of the IFN-beta gene. The 3.0 A crystal structure of the DNA-binding domains of ATF-2/c-Jun and two IRF-3 molecules in a complex with 31 base pairs (bp) of the PRDIV-PRDIII region of the IFN-beta enhancer shows that association of the four proteins with DNA creates a continuous surface for the recognition of 24 bp. The structure, together with in vitro binding studies and protein mutagenesis, shows that protein-protein interactions are not critical for cooperative binding. Instead, cooperativity arises mainly through nucleotide sequence-dependent structural changes in the DNA that allow formation of complementary DNA conformations. Because the binding sites overlap on the enhancer, the unit of recognition is the entire nucleotide sequence, not the individual subsites.

PubMed: 15510218
DOI: 10.1038/sj.emboj.7600453

Experimental method

X-RAY DIFFRACTION (3 Å)