The structure of apolipoprotein B100 from human low-density lipoprotein.

ABSTRACT: Low-density lipoprotein (LDL) has a central role in lipid and cholesterol metabolism and is a key agent in the development and progression of atherosclerosis, the leading cause of mortality worldwide^1,2. Apolipoprotein B100 (apoB100), one of the largest proteins in the genome, is the primary structural and functional component of LDL, yet its size and complex lipid associations have posed major challenges for structural studies³. Here we present the structure of apoB100 resolved to subnanometre resolution in most regions using an integrative approach of cryo-electron microscopy, AlphaFold2⁴ and molecular-dynamics-based refinement⁵. The structure consists of a large globular N-terminal domain and an approximately 61-nm-long continuous amphipathic

SUBMITTER: Berndsen ZT 

PROVIDER: S-EPMC11839476 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature