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Apolipoprotein a-i structural organization in high-density lipoproteins isolated from human plasma

Academic Article
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Overview

authors

  • Huang, R.
  • Silva, Ragd
  • Jerome, W. G.
  • Kontush, A.
  • Chapman, M. J.
  • Curtiss, Linda
  • Hodges, T. J.
  • Davidson, W. S.

publication date

  • 2011

journal

  • Nature Structural & Molecular Biology  Journal

abstract

  • High-density lipoproteins (HDLs) mediate cholesterol transport and protection from cardiovascular disease. Although synthetic HDLs have been studied for 30 years, the structures of human plasma-derived HDL and its major protein apolipoprotein apoA-I are unknown. We separated normal human HDL into five density subfractions and then further isolated those containing predominantly apoA-I (LpA-I). Using cross-linking chemistry and mass spectrometry, we found that apoA-I adopts a structural framework in these particles that closely mirrors that in synthetic HDL. We adapted established structures for synthetic HDL to generate the first detailed models of authentic human plasma HDL in which apoA-I adopts a symmetrical cage-like structure. The models suggest that HDL particle size is modulated by means of a twisting motion of the resident apoA-I molecules. This understanding offers insights into how apoA-I structure modulates HDL function and its interactions with other apolipoproteins.

subject areas

  • Apolipoprotein A-I
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Lipoproteins, HDL
  • Protein Conformation
  • Spectrometry, Mass, Electrospray Ionization
  • Tandem Mass Spectrometry
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Identity

PubMed Central ID

  • PMC3079355

International Standard Serial Number (ISSN)

  • 1545-9985

Digital Object Identifier (DOI)

  • 10.1038/nsmb.2028

PubMed ID

  • 21399642
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Additional Document Info

start page

  • 416

end page

  • 422

volume

  • 18

issue

  • 4

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