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The helix bundle: a reversible lipid binding motif Narayanaswami V; Kiss RS; Weers PMComp Biochem Physiol A Mol Integr Physiol 2010[Feb]; 155 (2): 123-33Apolipoproteins 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.|*Protein Folding[MESH]|*Protein Structure, Secondary[MESH]|Animals[MESH]|Apolipoproteins/*chemistry/metabolism[MESH]|Humans[MESH]|Lipid Metabolism[MESH]|Lipids/*chemistry[MESH]|Models, Molecular[MESH]|Protein Binding[MESH]|Protein Conformation[MESH] |
