Structural features contributing to the RARβ-selectivity and full agonistic activity of BMS948.

<p>(A) Structure superposition of BMS948-bound RARβ (violet) with Am580-bound RARα (blue). (B) Structure superposition of BMS411-bound RARβ (yellow) with BMS614-bound RARα (blue). (C) Structure superposition of BMS411-bound RARβ (yellow) with BMS948-bound RARβ (violet). (D) Superposition of the docking models of BMS411 (yellow) and BMS948 (violet) in RARα. (E) Structure superposition of BMS948-bound RARβ (violet) with BMS961-bound RARγ (green). (F) Superposition of all BMS-bound RARβ structures highlighting the differential positioning of the phenyl extensions relative to helix H12. Superposition of the structures was done using the SSM function in Coot[<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0123195#pone.0123195.ref033" target="_blank">33</a>].