Structural models of human apolipoprotein A-I: a critical analysis and review.
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 amphipathic alpha-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.
Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, AL 35294-0005, USA. christie@uab.edu
C G
CG
Brouillette
G M
GM
Anantharamaiah
J A
JA
Engler
D W
DW
Borhani
D000595:Amino Acid Sequence; D000818:Animals; D016632:Apolipoprotein A-I / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001161:Arteriosclerosis / Q000378:metabolism; D003461:Crystallography; D006801:Humans; D050356:Lipid Metabolism; D008075:Lipoproteins, HDL / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D013045:Species Specificity
D016632:Apolipoprotein A-I; D008075:Lipoproteins, HDL