Fig. 3: Mutational analysis of the p53-DBD/BCL-2 interactions.
From: Structures of p53/BCL-2 complex suggest a mechanism for p53 to antagonize BCL-2 activity
a Wild-type or mutant His-BCL-2 proteins were incubated with wild-type p53-DBD. The complex was immobilized by nickel beads and subjected to western blotting as indicated. b Wild-type GST-BCL-2 was incubated with wild-type or mutant p53-DBD. The complex was immobilized by glutathione sepharose and subjected to western blotting as indicated. c The binding affinity of wild-type GST-p53-DBD to BCL-2 mutants was analyzed by MST. d The binding affinity of GST-p53-DBD mutants to wild-type BCL-2 was analyzed by MST. Data are represented as the mean ± SD of n = 3 independent experiments. Curves were fitted, and KD values of interactions were calculated using experimental data with a KD model by MO. Affinity Assay software. Source data are provided as a Source Data file.
