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- W2010242022 abstract "Apolipoprotein (apo) B, the major protein component of the atherogenic low-density lipoprotein (LDL), has a pentapartite structure, NH2-βα1-β1-α2-β2-α3-COOH, the β domains containing multiple amphipathic β strands and the α domains containing multiple amphipathic α helixes. We recently reported that the first 1000 residues of human apoB-100 have sequence and amphipathic motif homologies to the lipid-pocket of lamprey lipovitellin (LV) [Segrest, J. P., Jones, M. K., and Dashti, N. (1999) J. Lipid Res. 40, 1401−1416]. The lipid-pocket of LV is a small triangular space lined by three antiparallel amphipathic β sheets, βA, βB, and βD. The βA and βB sheets are joined together by an antiparallel α helical bundle, α domain. We proposed [Segrest, J. P., Jones, M. K., and Dashti, N. (1999) J. Lipid Res. 40, 1401−1416] that formation of a LV-like lipid-pocket is necessary for lipid-transfer to apoB-containing lipoprotein particles and that this pocket is formed by association of the region of the βα1 domain homologous to the βA and βB sheets of LV with a βD-like amphipathic β sheet from microsomal triglyceride transfer protein (MTP). To test this hypothesis, we generated four truncated cDNA constructs terminating at or near the juncture of the βα1 and β1 domains: Residues 1−800 (apoB:800), 1−931 (apoB:931), 1−1000 (apoB:1000), and 1−1200 (apoB:1200). Characterization of particles secreted by stable transformants of the McA-RH7777 cell line demonstrated that (i) ApoB:800, missing the βB domain, was secreted as a lipid-poor aggregate. (ii) ApoB:931, containing most, but not all, of the βB domain, was secreted as lipid-poor particles unassociated with MTP. (iii) ApoB:1000, containing the entire βB domain, was secreted as a relatively lipid-rich particle associated hydrophobically with MTP. (iv) ApoB:1200, containing the βα1 domain plus 200 residues of the β1 domain, was secreted predominantly as a lipid-poor particle but also as a minor relatively lipid-rich, MTP-associated particle. We thus have captured an intermediate in apoB-containing particle assembly, a lipid transfer competent pocket formed by association of the complete βα1 domain of apoB with MTP." @default.
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- W2010242022 date "2002-05-09" @default.
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- W2010242022 title "The N-Terminal 1000 Residues of Apolipoprotein B Associate with Microsomal Triglyceride Transfer Protein to Create a Lipid Transfer Pocket Required for Lipoprotein Assembly" @default.
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- W2010242022 doi "https://doi.org/10.1021/bi011757l" @default.
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