Model of biologically active apolipoprotein E bound to dipalmitoylphosphatidylcholine
CA Peters-Libeu, Y Newhouse, DM Hatters, KH Weisgraber
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2006
Apolipoprotein (apo)E plays a critical role in cholesterol transport, through high affinity binding to the low density lipoprotein receptor. This interaction requires apoE to be associated with a lipoprotein particle. To determine the structure of biologically active apoE on a lipoprotein particle, we crystallized dipalmitoylphosphatidylcholine particles containing two apoE molecules and determined the molecular envelope of apoE at 10 Angstroms resolution. On the basis of the molecular envelope and supporting biochemical evidence, we propose a model in which each apoE molecule is folded into a helical hairpin with the binding region for the low density lipoprotein receptor at its apex.
Awarded by NATIONAL HEART, LUNG, AND BLOOD INSTITUTE
Awarded by NATIONAL INSTITUTE ON AGING
Awarded by NHLBI NIH HHS
Awarded by NIA NIH HHS