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Drug strategies for the prevention of the disease are largely centered on the interaction of low\u2010density lipoprotein receptor (LDLR) with the apolipoprotein B\u2010100 (apoB\u2010100) protein on low\u2010density lipoprotein (LDL). Recently, the structure of apoB\u2010100 on LDL was determined in the absence and presence of LDLR, using cryo\u2010electron microscopy. A remarkable structural feature of apoB\u2010100 is the lack of any significant tertiary structure within the C\u2010terminal two\u2010thirds of the protein (&gt;3000 residues). Instead, apoB\u2010100 forms amphipathic helices and \u03b2\u2010sheets on the phospholipid surface of LDL, which envelops its neutral lipid core. The apoB\u2010100 ligand binding domain for LDLR includes multiple points on a circumferential \u03b2\u2010belt and on the N terminus. In the course of this study, we also observed several instances of structural heterogeneity in apoB\u2010100. 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