Effects of p.Ala151Ser and p.Ile157Thr mutations in the predicted structure of human ALDH1A2. A) Cartoon representation of the ALDH1A2 monomer, highlighting p.Ala151Ser (orange arrowhead) and p.Ile157Thr (red arrowhead) mutations. B-C) Surface mode views of wild type Aldh1A2 dimers. D) The boxed structure highlights homodimer surfaces that take part in the process of tetramerization. E-I) Hetero- and homodimer Aldh1A2 configurations produced in homozygote and heterozygote individuals for the p.Ala151Ser and p.Ile157Thr mutations. Wild type and mutant homo- and heterodimer tetramerization surfaces are represented as in D. The asterisk indicates the major conformational changes observed in the tetramerization domains of p.Ala151Ser (orange) and p.Ile157Thr (red) mutants in homo or heterodimer configurations. J) Homotetramer model of wild type human Aldh1A2. K) 90° rotated Y axis view of the wild type human Aldh1a2 homotetramer as shown in J. L) Ile157Thr-wild type heterotetramer showing large areas of stereo chemical hindrance. M) p.Ala151Ser-wild type heterotetramers showing minor departures from the wild type conformation.