Structural basis of dysfunctional apolipoprotein-induced dyslipidemia

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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.