Fig. 3: Biochemical and structural characterizations of the interactions of ATG16L1 FIR with mammalian ATG8 family proteins.

a ITC-based measurement of the binding affinity of GABARAPL1 with Trx-tagged ATG16L1 FIR. b Ribbon diagram showing the overall structure of the GABARAPL1/ATG16L1 FIR complex. In this drawing, the GABARAPL1 molecule is colored in green, while ATG16L1 FIR in magenta. c The ribbon-stick model showing the detailed interactions between GABARAPL1 and ATG16L1 FIR. The hydrogen bonds and salt bridges involved in the interaction are shown as dotted lines. d The combined surface charge representation and the ribbon-stick model showing the charge-charge interactions between GABARAPL1 and ATG16L1 FIR. e The combined surface representation and the ribbon-stick model showing the hydrophobic interactions between GABARAPL1 and ATG16L1 FIR. In this drawing, ATG16L1 FIR is displayed in the ribbon-stick model, and GABARAPL1 is shown in surface representation, colored by different amino acid types. Specifically, the hydrophobic amino acid residues in the surface model of GABARAPL1 are drawn in yellow; the positively charged residues are drawn in blue; the negatively charged residues are drawn in red, and the uncharged polar residues are drawn in gray.