Figure 1 | Scientific Reports

Figure 1

From: Dynamical Binding Modes Determine Agonistic and Antagonistic Ligand Effects in the Prostate-Specific G-Protein Coupled Receptor (PSGR)

Figure 1

Structure of α-ionones and β-ionone, and the predicted ligand binding cavity. (R)- α-ionone in cyan, (S)- α-ionone in dark blue, β-ionone in orange. (a) Chemical structures and 3D structures of ionones after overlay of their ring moieties. The main difference between the three isoforms lies in the angle of the butenoneyl side chain to the ring moiety. (b) PSGR structural model with a close-up of the central binding site. Protein backbone in grey, β-ionone in its best docking posture in the inactive protein state in orange sticks, surrounding mutated residues in blue sticks. Helices numbered in roman numbers. The displayed structure is the initial inactive protein model used for ligand docking. Mutation of all displayed residues had an effect on ligand binding and protein activation (see Table 1). We therefore propose this position within the protein model as the β-ionone binding site.

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