Journal
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR & INTEGRATIVE PHYSIOLOGY
Volume 155, Issue 2, Pages 123-133Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cbpa.2009.09.009
Keywords
Apolipophorin; Apolipoprotein; Lipophorin; Lipoprotein; Protein structure; Cholesterol; Diacylglycerol; Triacylglycerol
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Funding
- NIH [R15 HL077135]
- SCORE [GM 063119]
- CIHR [MOP-89972]
- American Heart Association [07551374]
- CSULB SCAC Award
- Tobacco-Related Disease Research Program [17 RT-0165]
- Drake Family Trust (VN)
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Apolipoproteins are the protein components of lipoproteins that have the innate ability to inter convert between a lipid-free and a lipid-bound form in a facile manner, a remarkable property conferred by the helix bundle motif Composed of a series of four or five amphipathic alpha-helices that fold to form a helix bundle, this motif allows the en face orientation of the hydrophobic faces of the alpha-helices in the protein interior in the lipid-free state. A conformational switch then permits helix-helix interactions to be substituted by helix-lipid interactions upon lipid binding interaction. This review compares the apolipoprotein high-resolution structures and the factors that trigger this switch in insect apolipophorin III and the mammalian apolipoproteins, apolipoprotein E and apolipoprotein A-I, pointing out the commonalities and key differences in the mode of lipid interaction. Further insights into the lipid-bound conformation of apolipoproteins are required to fully understand their functional role under physiological conditions. (C) 2009 Elsevier Inc. All rights reserved.
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