2O61

Crystal Structure of NFkB, IRF7, IRF3 bound to the interferon-b enhancer

Summary for 2O61

• Entry DOI: 10.2210/pdb2o61/pdb
• Related: 2O6G
• Descriptor: 36-MER, 34-MER, Transcription factor p65/Interferon regulatory factor 7/Interferon regulatory factor 3 fusion protein, ... (5 entities in total)
• Functional Keywords: protein-dna complex, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : Q14653; Nucleus: P19838
• Total number of polymer chains: 4
• Total formula weight: 117736.90

Authors

Panne, D. (deposition date: 2006-12-06, release date: 2007-07-24, Last modification date: 2023-12-27)

Primary citation

Panne, D.,Maniatis, T.,Harrison, S.C.
An Atomic Model of the Interferon-beta Enhanceosome.
Cell(Cambridge,Mass.), 129:1111-1123, 2007

PubMed Abstract: Transcriptional activation of the interferon-beta (IFN-beta) gene requires assembly of an enhanceosome containing ATF-2/c-Jun, IRF-3/IRF-7, and NFkappaB. These factors bind cooperatively to the IFN-beta enhancer and recruit coactivators and chromatin-remodeling proteins to the IFN-beta promoter. We describe here a crystal structure of the DNA-binding domains of IRF-3, IRF-7, and NFkappaB, bound to one half of the enhancer, and use a previously described structure of the remaining half to assemble a complete picture of enhanceosome architecture in the vicinity of the DNA. Association of eight proteins with the enhancer creates a continuous surface for recognizing a composite DNA-binding element. Paucity of local protein-protein contacts suggests that cooperative occupancy of the enhancer comes from both binding-induced changes in DNA conformation and interactions with additional components such as CBP. Contacts with virtually every nucleotide pair account for the evolutionary invariance of the enhancer sequence.

PubMed: 17574024
DOI: 10.1016/j.cell.2007.05.019

Experimental method

X-RAY DIFFRACTION (2.8 Å)