The structure of dimeric apolipoprotein A-IV and its mechanism of self-association.

Structure
Xiaodi DengThomas B Thompson

Abstract

Apolipoproteins are key structural elements of lipoproteins and critical mediators of lipid metabolism. Their detergent-like properties allow them to emulsify lipid or exist in a soluble lipid-free form in various states of self-association. Unfortunately, these traits have hampered high-resolution structural studies needed to understand the biogenesis of cardioprotective high-density lipoproteins (HDLs). We derived a crystal structure of the core domain of human apolipoprotein (apo)A-IV, an HDL component and important mediator of lipid absorption. The structure at 2.4 Å depicts two linearly connected 4-helix bundles participating in a helix swapping arrangement that offers a clear explanation for how the protein self-associates as well as clues to the structure of its monomeric form. This also provides a logical basis for antiparallel arrangements recently described for lipid-containing particles. Furthermore, we propose a "swinging door" model for apoA-IV lipid association.

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Citations

Oct 11, 2015·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·J Roman-PadillaM Manchado
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Feb 3, 2015·Journal of Lipid Research·Fei WangPatrick Tso
Jan 5, 2013·The Journal of Biological Chemistry·Xiaodi DengThomas B Thompson
Mar 4, 2015·The Journal of Biological Chemistry·Xiaodi DengThomas B Thompson
Aug 30, 2019·Journal of Lipid Research·Hideru ObinataTimothy Hla
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Nov 16, 2020·Biochimica Et Biophysica Acta. Biomembranes·Andreas Haahr LarsenSøren Roi Midtgaard

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