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.
© 2004-2018 中国地质图书馆版权所有 京ICP备05064691号 京公网安备11010802017129号 地址:北京市海淀区学院路29号 邮编:100083 电话:办公室:(+86 10)66554848;文献借阅、咨询服务、科技查新:66554700 |