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Novel RAR antagonists. (A and B) Stereo representation of antagonists 1 and 2 docked into the binding site of the receptor. The ligands make extensive hydrophobic interactions with residues from helix 3, helix 5, and helix 11. Antagonist 2 (B) is engaged in an additional hydrogen bond with Ser-234 of helix 3 and contacts the remodeled C terminus (red) at Pro-405. (C and D) The fit of antagonists 1 and 2 into the receptor binding pocket is shown.
