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

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• 作者：Brouillette ; Christie G. ; Anantharamaiah ; G.M. ; Engler ; Jeffrey A. ; Borhani ; David W.
• 关键词：Apolipoprotein A-I mutant ; High density lipoprotein ; Exchangeable apolipoprotein ; Apolipoprotein E ; Apolipophorin III ; Molten globule ; HDL model ; Lipid binding ; Protein folding
• 刊名：Biochimica et Biophysica Acta (BBA)/Molecular and Cell Biology of Lipids
• 出版年：2001
• 出版时间：March 30, 2001
• 年：2001
• 卷：1531
• 期：1-2
• 页码：4-46
• 全文大小：1.51 M

文摘

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.