Fig. 3

apoA-V multiple sequence alignment and schematic structure. A Sequence alignment of apoA-V from multiple species, from top to bottom: human (HUMAN) wild-type apoA-V, mutated human apoA-V, rat (RAT), mouse (MOUSE), Hawaiian monk seal (NEOSC), cheetah (ACIJB), and harbor seal (PHOVI). B Schematic diagram of apoA-V showing its main domains and APOA5 mutations. Signal peptide (Met1–Ala23). α-Helical structures (Ala112–Val153, Leu173–Val213, Pro221–Ala262, Gln275–Leu314). Lipid binding domains (Arg24–Val169, Tyr194–Gly268, Pro316–Pro366). Receptor binding domains (Thr21–Gly26, Gly36–Gln43, Lys48–Ala54, Val90–Glu98, Glu146–Arg152, His182–Leu190, Ser232–Leu237, Asp251–Leu257, Val281–Thr292). Heparin binding domain (Leu209–Leu250). LPL activation domain (Pro215–Phe261). C Predicted tertiary structure of wild-type apoA-V and pathogenic mutations. The structure of wild-type apoA-V is depicted in the center. The yellow part represents the signal peptide, the green part is the lipid binding domain, the red part is the LPL activation domain. W1–4 indicates wild-type 1–4. Mutations 1–4 (M1–4) represents the predicted tertiary structure of p.S35N, p.D167V, p.G185C, p.K188I, p.R223C