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• W2009011878 abstract "The ‘POU’ (acronym of Pit-1, Oct-1, Unc-86) family of transcription factors share a common DNA-binding domain of approximately 160 residues, comprising so-called ‘POUs’ and ‘POUh’ sub-domains connected by a flexible linker. The importance of POU proteins as developmental regulators and tumor-promoting agents is due to linker flexibility, which allows them to adapt to a considerable variety of DNA targets. However, because of this flexibility, it has not been possible to determine the Oct-1/Pit-1 linker structure in crystallographic POU/DNA complexes. We have previously shown that the neuronal POU protein N-Oct-3 linker contains a structured region. Here, we have used a combination of hydrodynamic methods, DNA footprinting experiments, molecular modeling and small angle X-ray scattering to (i) structurally interpret the N-Oct-3-binding site within the HLA DRα gene promoter and deduce from this a novel POU domain allosteric conformation and (ii) analyze the molecular mechanisms involved in conformational transitions. We conclude that there might exist a continuum running from free to ‘pre-bound’ N-Oct-3 POU conformations and that regulatory DNA regions likely select pre-existing conformers, in addition to molding the appropriate DBD structure. Finally, we suggest that a specific pair of glycine residues in the linker might act as a major conformational switch." @default.
• W2009011878 created "2016-06-24" @default.
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• W2009011878 date "2007-06-18" @default.
• W2009011878 modified "2023-10-11" @default.
• W2009011878 title "Fine-tuning of intrinsic N-Oct-3 POU domain allostery by regulatory DNA targets" @default.
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• W2009011878 doi "https://doi.org/10.1093/nar/gkm453" @default.
• W2009011878 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1935007" @default.
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• W2009011878 hasPublicationYear "2007" @default.
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