Christie G. Brouillette، نويسنده , , G. M. Anantharamaiah، نويسنده , , Jeffrey A. Engler، نويسنده , , Alexandre P. Kuzin and David W. Borhani، نويسنده ,

1601742

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

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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 amphiphatic α-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.

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Exchangeable apolipoprotein , apolipoprotein E , molten globule , Apolipoprotein A-I mutant , lipid binding , HDL model , high density lipoprotein , Apolipophorin III , protein folding

Studia Iranica

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