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• W3100822419 startingPage "183495" @default.
• W3100822419 abstract "Apolipoproteins are vital to lipid metabolism and cholesterol transport in the human body. Here we present a structural study of the lipid-bound particles formed by ApoE3 in a full-length and a truncated version. The particles are formed with, respectively, POPC and DMPC and investigated by small-angle X-ray scattering and negative stain electron microscopy. We find that lipid-bound ApoE3 particles are elliptical, disc-shaped particles composed of a central lipid bilayer encircled by two amphipathic ApoE3 proteins. We went on to investigate a truncated form of ApoE3 containing only residue 80 to 255 (ApoE3 80–255 ), which is the central helical repeat segment of ApoE3. The lipid-bound ApoE3 80–255 particles are found to have the same morphology as the particles with full-length ApoE3. However, they are larger, and form more heterogeneous discoidal structures with four proteins per particle. This behavior is in contrast to ApoA1 where the highly similar helical repeat domain determines the size and stoichiometry of the formed particles both in the case of full-length and truncated ApoA1. Our data hence points towards different mechanisms for lipid bilayer structural modulation by ApoA1 and ApoE3 due to different roles of the non-repeat segments. • Lipid-bound ApoE3 forms discoidal particles. • Unlike in ApoA1, the central helical repeat region of ApoE3 is not the sole domain for forming discoidal lipid particles. • The central helical repeat region of ApoE3 form lipid-bound discoidal particles with four copies of the protein." @default.
• W3100822419 created "2020-11-23" @default.
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• W3100822419 date "2021-01-01" @default.
• W3100822419 modified "2023-09-24" @default.
• W3100822419 title "Lipid-bound ApoE3 self-assemble into elliptical disc-shaped particles" @default.
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• W3100822419 doi "https://doi.org/10.1016/j.bbamem.2020.183495" @default.
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