Structure and function of apolipoprotein A-I and high-density lipoprotein.
Structural biology and molecular modeling have provided intriguing insights into the atomic details of the lipid-associated structure of the major protein component of HDL, apo A-I. For the first time, an atomic resolution map is available for future studies of the molecular interactions of HDL in such biological processes as ABC1-regulated HDL assembly, LCAT activation, receptor binding, reverse lipid transport and HDL heterogeneity. Within the context of this paradigm, the current review summarizes the state of HDL research.
Segrest
J P
JP
Department of Medicine, UAB Medical Center, Birmingham, Alabama 35294-0012, USA. segrest@uab.edu
Li
L
L
Anantharamaiah
G M
GM
Harvey
S C
SC
Liadaki
K N
KN
Zannis
V
V
D000818:Animals; D016632:Apolipoprotein A-I / Q000737:chemistry* / Q000502:physiology*; D002784:Cholesterol / Q000378:metabolism; D006801:Humans; D008074:Lipoproteins / Q000737:chemistry; D008075:Lipoproteins, HDL / Q000737:chemistry* / Q000502:physiology*; D051379:Mice; D008958:Models, Molecular; D011487:Protein Conformation
D016632:Apolipoprotein A-I; D008074:Lipoproteins; D008075:Lipoproteins, HDL; C034366:discoidal lipoproteins; D002784:Cholesterol