Fig. 3.

Effects of mutations at RARβ DBD–LBD interface on the transcription and DNA binding of RARβ–RXRα heterodimer. a Functional reporter assays testing the transcriptional activities of RARβ–RXRα. The wide-type (WT) RARβ and its mutants (majority at the interface) were tested for their transactivation on DR1 ANGPTL4 (left) and DR5 CYP26A1 (right) reporters, in the absence or presence of 1 μM REA. Each sample represents the average reading of cells from three wells, and data are shown as mean ± SD. The statistical differences between mutants (or the empty vector) and corresponding WT were calculated using the two-tailed t-test (*P < 0.05; **P < 0.01). b DNA-binding affinities of RARβ–RXRα heterodimer (WT and RARβ mutants) to DR1 DNA (left) and DR5 DNA (right) measured in the presence of REA and 9CR at 3× concentrations. K _D values are in parentheses. The data points are plotted as mean ± SD from three technical replicates respectively