2I9T

Structure of NF-kB p65-p50 heterodimer bound to PRDII element of B-interferon promoter

Summary for 2I9T

• Entry DOI: 10.2210/pdb2i9t/pdb
• Descriptor: 5'-D(*AP*GP*TP*GP*GP*GP*AP*AP*AP*TP*TP*CP*CP*TP*CP*TP*G)-3', 5'-D(*CP*AP*GP*AP*GP*GP*AP*AP*TP*TP*TP*CP*CP*CP*AP*CP*T)-3', Transcription factor p65, ... (5 entities in total)
• Functional Keywords: protein-dna complex, transcription-dna complex, transcription/dna
• Biological source: Mus musculus (house mouse); More
• Cellular location: Nucleus : Q04207; Nucleus. Isoform 5: Cytoplasm. Isoform 6: Nucleus. Isoform 7: Nucleus: P25799
• Total number of polymer chains: 4
• Total formula weight: 77102.62

Authors

Escalante, C.R.,Shen, L.,Thanos, D.,Aggarwal, A.K. (deposition date: 2006-09-06, release date: 2007-02-06, Last modification date: 2024-02-21)

Primary citation

Escalante, C.R.,Shen, L.,Thanos, D.,Aggarwal, A.K.
Structure of NF-kappaB p50/p65 heterodimer bound to the PRDII DNA element from the interferon-beta promoter
Structure, 10:383-391, 2002

PubMed Abstract: Upon viral infection, NF-kappaB translocates to the nucleus and activates the IFN-beta gene by binding to the PRDII element. Strikingly, NF-kappaB loses its ability to activate the IFN-beta gene when the PRDII element is substituted by closely related sites. We report here the crystal structure of NF-kappaB p50/p65 heterodimer bound to the PRDII element from the IFN-beta promoter. The structure reveals an unexpected alteration in configuration, in which the p50 specificity domain moves by as much as approximately 9 A when compared to NF-kappaB heterodimer bound to the immunoglobulin kappaB site (Ig-kappaB) while maintaining the same base-specific contacts with the DNA. Taken together, the structure offers new insights into the allosteric effects of closely related DNA sites on the configuration of NF-kappaB and its transcriptional selectivity.

PubMed: 12005436
DOI: 10.1016/S0969-2126(02)00723-2

Experimental method

X-RAY DIFFRACTION (2.8 Å)