Fig. 3

Fig. 3

AlphaFold2 modeling of PKHD1L1 protein fragments carrying p.(Gly120Ser) and p.(Gly1314Val) mutations. a Superposed AlphaFold2 models of both native Hs IPT1-2 (orange) and Hs IPT1-2 p.(Gly120Ser) variant (mauve) are shown. b Higher magnification image of the mutated site. p.S129 in lime and p.G129 in cyan. No apparent structural changes are predicted by AlphaFold2. c Structural model of Hs IPT5-6 showing the native p.Gly1314 position. d Superposed Hs IPT5-6 (orange) and Hs IPT5-6 p.(Gly1314Val) (mauve) structures showing a structural change predicted by AlphaFold2 as a result of p.(Gly1314Val) substitution. β-strands and loops do not overlap, with a dashed black arrow reporting the loop shift. e Higher magnification image of the mutated site showing the conformation change of β-strands and loops. p.V1314 (lime) causes steric hindrance in the area inducing an expanded conformation to the variant structure in mauve. See dashed arrows