2PI0

Crystal Structure of IRF-3 bound to the PRDIII-I regulatory element of the human interferon-B enhancer

Summary for 2PI0

• Entry DOI: 10.2210/pdb2pi0/pdb
• Descriptor: PRDIII-I region of human interferon-B promoter strand 1, PRDIII-I region of human interferon-B promoter strand 2, Interferon regulatory factor 3, ... (4 entities in total)
• Functional Keywords: interferon, protein-dna complex, transcription, transcription activator-dna complex, transcription activator/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: 2PI0
• Total number of polymer chains: 6
• Total formula weight: 73272.20

Authors

Escalante, C.R.,Nistal-Villan, E.,Leyi, S.,Garcia-Sastre, A.,Aggarwal, A.K. (deposition date: 2007-04-12, release date: 2007-10-30, Last modification date: 2023-08-30)

Primary citation

Escalante, C.R.,Nistal-Villan, E.,Shen, L.,Garcia-Sastre, A.,Aggarwal, A.K.
Structure of IRF-3 bound to the PRDIII-I regulatory element of the human interferon-beta enhancer.
Mol.Cell, 26:703-716, 2007

PubMed Abstract: Interferon regulatory factor 3 (IRF-3) is a key transcription factor in the assembly of the mammalian interferon-beta (IFN-beta) enhanceosome. We present here the structure of IRF-3 DNA binding domain in complex with the complete PRDIII-I regulatory element of the human IFN-beta enhancer. We show that four IRF-3 molecules bind in tandem to, variably spaced, consensus and nonconsensus IRF sites on the composite element. The ability of IRF-3 to bind these variable sites derives in part from two nonconserved arginines (Arg78 and Arg86) that partake in alternate protein-DNA contacts. We also show that the protein-DNA contacts are highly overlapped and that all four IRF sites are required for gene activation in vivo. In addition, we show that changing the nonconsensus IRF sites to consensus sites creates a more efficient enhancer in vivo. Together, the structure and accompanying biological data provide insights into the assembly of the IFN-beta enhanceosome in mammals.

PubMed: 17560375
DOI: 10.1016/j.molcel.2007.04.022

Experimental method

X-RAY DIFFRACTION (2.31 Å)