Fig. 5: Molecular docking of formyl peptides.
From: Structural basis of ligand binding modes at the human formyl peptide receptor 2
a Docking model of FPR2-fMLF. The receptor is shown in cyan cartoon representation. The peptide fMLF and the FPR2 residues that may form interactions with fMLF are shown as sticks and colored magenta and blue, respectively. Salt bridges and hydrogen bonds are shown as red and green dashed lines, respectively. b Docking poses of fMLF, fMLFK, and fMLFII in comparison with the binding pose of WKYMVm in FPR2. The peptides WKYMVm, fMLF, fMLFK, and fMLFII are shown as orange, magenta, yellow, and gray sticks, respectively. c Comparison of the fMLF docking poses in FPR1 and FPR2. The model of FPR1-fMLF is colored light green (FPR1) and green (fMLF), while the model of FPR2-fMLF is in cyan (FPR2) and magenta (fMLF). The residues that may form salt-bridge interactions with the C-terminal COO− group of fMLF are shown as sticks and colored light green (R842.63 and K852.64 in FPR1) and blue (R2015.38 and R2055.42 in FPR2). The salt bridges are displayed as black and red dashed lines in FPR1 and FPR2, respectively. d Docking pose of fMLFK in FPR2. fMLFK is shown as yellow sticks. The receptor residues that may form polar interactions with the peptide residue K4 are shown as blue sticks. The polar interactions are shown as red (salt bridge) and green (hydrogen bond) dashed lines. e Docking pose of fMLFII in FPR2. fMLFII is shown as gray sticks. The receptor residues that may form hydrophobic interactions with the peptide residues I4 and I5 are shown as blue sticks.
