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. 2021 Feb 23;62:100054. doi: 10.1016/j.jlr.2021.100054

Fig. 3.

Fig. 3

Acyl chain-dependent difference in the binding models of 2-monoacylglycerols to cellular retinol binding protein 2 (CRBP2). A: Ribbon representation of the overlay structures of CRBP2 [Protein Data Bank (PDB): 7JWR]. Position of 2-oleoyl glycerol in the binding pocket (light red transparent surface) is indicated by the model representation of the ligand. The portal region of the protein is colored blue and labeled with corresponding secondary structures. B: Superimposed structures of CRBP2 in complex with 2-arachidonoylglycerol (2-AG) (colored blue) (PDB: 6BTH), 2-oleoyl glycerol (purple) (PDB: 7WR), and 2-linoleoyl glycerol (green) (PDB: 7JWD). The overlapping ends of fatty acid chains are marked with yellow arrow. The difference in the spatial positions of the chain between these monoacylglycerols is marked with red arrow. C: Comparison of the positions of 2-AG (blue) and 2-palmitoylglycerol (2-PG) (orange) (PDB: 7JX2) in the binding site. D: Orientation of the acyl chains of 2-AG and 2-lauroyl-glycerol (2-LaG) (light blue) (PDB: 7K3I) in relation to the side chain of Y60. Regardless the differences in the orientation of the acyl chains inside the binding pocket of CRBP2, both ligands cause repositioning of the Y60 side chain as compared with the apoform of the protein.