David Auble
The interferon-beta enhanceosome is a multisubunit protein-DNA complex that directs transcriptional activation of the IFN-beta gene. By combining structures of different proteins bound to their cognate DNA sites, Panne et al. (Cell 129:1111 (2007)) derived a structural model for all of the enhancer binding proteins bound to the DNA simultaneously. What one can see in the images below is that the proteins form a nearly continuous surface for DNA recognition. However, there are relatively few interactions between the different protein constituents. Note that these are the structures of the DNA binding domains, not the complete proteins, so protein-protein interactions may be mediated by other domains not shown. Binding may also be stabilized by cooperative interactions with other co-activator proteins that are not shown in this model. The authors suggest that cooperativity also derives from binding-induced changes in DNA conformation. The pdb file for this composite structure was published by the authors as supplementary data.
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RelA p50 IRF-7D IRF3C IRF7B IRF3A c-Jun ATF-2
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