2pi0
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Crystal Structure of IRF-3 bound to the PRDIII-I regulatory element of the human interferon-B enhancer
OverviewOverview
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.
About this StructureAbout this Structure
2PI0 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of IRF-3 bound to the PRDIII-I regulatory element of the human interferon-beta enhancer., Escalante CR, Nistal-Villan E, Shen L, Garcia-Sastre A, Aggarwal AK, Mol Cell. 2007 Jun 8;26(5):703-16. PMID:17560375
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