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Here, we unveil that the structured DNA\u2010binding domain (DBD) of a TF acts as an entropic switch to regulate the release of the intrinsically disordered region (IDR). Using high\u2010resolution solution NMR spectroscopy, we demonstrate that DNA binding significantly shifts the conformational equilibrium of the DBD toward a highly dynamic state. This conformational shift allosterically triggers the release of the IDR, thereby promoting macroscopic biomolecular condensation via multivalent interactions between the IDR and other molecules. 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