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  • 标题:Structure of apolipoprotein B-100 in low density lipoproteins
  • 本地全文:下载
  • 作者:Jere P. Segrest ; Martin K. Jones ; Hans De Loof
  • 期刊名称:JLR Papers In Press
  • 印刷版ISSN:0022-2275
  • 电子版ISSN:1539-7262
  • 出版年度:2001
  • 卷号:42
  • 期号:9
  • 页码:1346-1367
  • 语种:English
  • 出版社:American Society for Biochemistry and Molecular Biology
  • 摘要:There is general consensus that amphipathic α-helices and β sheets represent the major lipid-associating motifs of apolipoprotein (apo)B-100. In this review, we examine the existing experimental and computational evidence for the pentapartite domain structure of apoB. In the pentapartite nomenclature presented in this review (NH2-βα 11223-COOH), the original α1 globular domain (Segrest, J. P. et al. 1994. Arterioscler. Thromb. 14: 1674–1685) is expanded to include residues 1–1,000 and renamed the βα 1 domain. This change reflects the likelihood that the βα 1 domain, like lamprey lipovitellin, is a globular composite of α-helical and β-sheet secondary structures that participates in lipid accumulation in the co-translationally assembled prenascent triglyceride-rich lipoprotein particles. Evidence is presented that the hydrophobic faces of the amphipathic β sheets of the β1 and β2 domains of apoB-100 are in direct contact with the neutral lipid core of apoB-containing lipoproteins and play a role in core lipid organization. Evidence is also presented that these β sheets largely determine LDL particle diameter. Analysis of published data shows that with a reduction in particle size, there is an increase in the number of amphipathic helices of the α2 and α3 domains associated with the surface lipids of the LDL particle; these increases modulate the surface pressure decreases caused by a reduction in radius of curvature. The properties of the LDL receptor-binding region within the overall domain structure of apoB-100 are also discussed. Finally, recent three-dimensional models of LDL obtained by cryoelectron microscopy and X-ray crystallography are discussed. These models show three common features: a semidiscoidal shape, a surface knob with the dimensions of the βC globular domain of lipovitellin, and planar multilayers in the lipid core that are approximately 35 Å apart; the multilayers are thought to represent cholesteryl ester in the smectic phase. These models present a conundrum: are LDL particles circulating at 37°C spheroidal in shape, as generally assumed, or are they semidiscoidal in shape, as suggested by the models? The limited evidence available supports a spheroidal shape. —Segrest, J. P., M. K. Jones, H. De Loof, and N. Dashti. Structure of apolipoprotein B-100 in low density lipoproteins. J. Lipid Res. 2001. 42: 1346–1367.
  • 关键词:amphipathic β sheets ; amphipathic α-helices ; cryoelectron microscopy ; X-ray crystallography ; boundary lipid ; smectic phase ; lipid phase transition ; LDL receptor-binding domain
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