Structural models of human apolipoprotein A-I: a critical analysis and review.

Academic Article

Abstract

  • Human apolipoprotein (apo) A-I has been the subject of intense investigation because of its well-documented anti-atherogenic properties. About 70% of the protein found in high density lipoprotein complexes is apo A-I, a molecule that contains a series of highly homologous amphipathic alpha-helices. A number of significant experimental observations have allowed increasing sophisticated structural models for both the lipid-bound and the lipid-free forms of the apo A-I molecule to be tested critically. It seems clear, for example, that interactions between amphipathic domains in apo A-I may be crucial to understanding the dynamic nature of the molecule and the pathways by which the lipid-free molecule binds to lipid, both in a discoidal and a spherical particle. The state of the art of these structural studies is discussed and placed in context with current models and concepts of the physiological role of apo A-I and high-density lipoprotein in atherosclerosis and lipid metabolism.
  • Published In

    Keywords

  • Amino Acid Sequence, Animals, Apolipoprotein A-I, Arteriosclerosis, Crystallography, Humans, Lipid Metabolism, Lipoproteins, HDL, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Sequence Alignment, Species Specificity
  • Authorlist

  • Brouillette CG; Anantharamaiah GM; Engler JA; Borhani DW
  • Start Page

  • 4
  • End Page

  • 46
  • Volume

  • 1531
  • Issue

  • 1-2