Structural basis of dysfunctional apolipoprotein-induced dyslipidemia

为了探索导致低脂蛋白血症和系统性淀粉样变性的载脂蛋白天然突变的结构效应，我们检测了载脂蛋白A-I和E变体的三级结构、稳定性、脂质结合特性和聚集倾向。结果表明，突变引起的载脂蛋白N端螺旋束和C端螺旋结构的破坏导致疾病的严重后果。

To probe the structural effects of naturally occurring mutations of apolipoproteins that lead to hypolipoproteinemia and systemic amyloidosis, we examined the tertiary structure, stability, lipid-binding property, and aggregation propensity of apolipoprotein A-I and E variants. The results indicate that the disruption of the N-terminal helix bundle and the C-terminal helical structure in apolipoproteins caused by the mutations leads to the critical outcomes of diseases.