AhR- G1661A causes an arginine to lysine substitution in the acidic sub-domain of AhR-TAD with controversial phenotypic results.
We investigated the possible effects by multiple in silico analysis.
Secondary structure, solvent accessibility and pattern of the binding site and post translational modification predicted to be changed in the region.
The predicted changes may alter the interactions of TAD, especially with TATA-binding protein.
The flexibility of TAD could act as a moderating factor and causes distinct outcomes.