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. 2026 Mar 26;113(5):1090–1107. doi: 10.1016/j.ajhg.2026.03.002

Figure 2.

Figure 2

In silico structural analysis of ATG12 variants illustrating the effect on complex formation

(A) AlphaFold prediction of ATG12 structure (AlphaFold:O98417), in orthogonal views. Insets: position of p.Tyr120Ser (Y120S) variant in the ubiquitin fold of ATG12 is shown in purple. Position of p.Ala138Val (A138V) variant is shown in blue. Position of the p.Phe108L (F108L) variant is shown in yellow.

(B) Reported crystal structure of the ATG12-ATG5-ATG16N-ATG3 complex (PDB: 4NAW) showing the proximity of the two missense variants in this study to the interface between ATG12 and ATG5.

(C) Comparison of the existing crystal structure of the ATG12-ATG5-ATG16N-ATG3 complex and our expanded AlphaFold model with the two missense variants annotated in pink. The expanded AlphaFold model shows the full-length ATG3 sequence (yellow) wrapped around ATG12 (green), placing the variants in close proximity to the interfaces with both ATG5 and ATG3.