Figure 1 | Scientific Reports

Figure 1

From: Atomistic simulations shed new light on the activation mechanisms of RORγ and classify it as Type III nuclear hormone receptor regarding ligand-binding paths

Figure 1

(A) Overall structure of the RORγ-LBD with compound 5 bound in the orthosteric site (represented as CPK, in purple). The most important α-helices are labeled in red, as is the agonist lock H-bond formed between H479 (H11, in yellow) and Y502 (H12, in pink), shaping the co-activator docking site. The co-activator protein is docked on the lower part of the LBD (colored green). (B) 2D structures of representative compounds with activity on RORγ. Agonists: compounds 1-5 on top; Inverse agonists and antagonists on the bottom: compounds 6-12; 6-7 are found in complex with LBD and co-repressor. 8-9 are found in complex with LBD and neither co-activator nor co-repressor. 10-12 are found in complex with co-activator and feature water molecules in the interior of LBD next to H12; 10 breaks the agonist lock whereas 11-12 do not. The 2D structures are tagged with their respective Protein Data Bank entries, where each compound can be studied in complex with RORγ-LBD. The two MMPs simulated in this study are highlighted in the blue boxes: compounds 5 vs 10 and 4 vs 9.

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