Figure 2 - full size

 

Figure 2.
Co-crystal structure of human RBP4 with A1120. A, overall view of A1120-bound RBP4 structure. The RBP4 protein is shown in schematic representation with a spectrum color from blue (N terminus) to red (C terminus). A1120 is shown in stick representation with magenta for carbon atoms, red for oxygen atoms, blue for nitrogen atoms, and pale cyan for fluorine atoms. The 2f[o] - f[c] electron density map, contoured at 1σ, for A1120 is shown in gray mesh. B, protein-ligand interactions for A1120. The protein is shown in both stick (spectrum color) and molecular surface (wheat color) representations. The hydrogen bonds between RBP4 and A1120 are shown as black dashed lines. C, superposition of the A1120-RBP4 co-crystal structure and retinol-RBP4 co-crystal structure (PDB code: 1RBP). The carbon atoms are colored in gray for the retinol-bound structure. D, superposition of the A1120-RBP4 co-crystal structure on the RBP4·TTR complex structure (PDB code: 1QAB). The TTR tetramer is shown in molecule surface representation. The RBP4 proteins are shown in schematic representation with the RBP4 protein shown in gray in the TTR complex and in spectrum color in the A1120-bound form.

The above figure is reprinted by permission from the ASBMB: J Biol Chem (2009, 284, 7673-7680) copyright 2009.