A Characteristic Back Support Structure in the Bisphenol A-Binding Pocket in the Human Nuclear Receptor ERRγ
Figure 2
The homologous competitive binding assays between [3H]bisphenol A and non-labeled bisphenol A for the wild-type ERRγ-LBD and its mutants.
The receptors used were the wild-type ERRγ and its mutant receptors. (A) Leu342-substituted ERRγ mutant receptors, (B) Leu345-substituted ERRγ mutant receptors, (C) Asn346-substituted ERRγ mutant receptors, and (D) Ile349-substituted ERRγ mutant receptors. The graphs show representative dose-dependent binding curves, which give the IC50 value closest to the mean IC50 from at least three independent experiments.