Model of biologically active apolipoprotein E bound to dipalmitoylphosphatidylcholine.
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.
Peters-Libeu
Clare A
CA
Gladstone Institute of Cardiovascular Disease and Gladstone Institute of Neurological Disease, San Francisco, CA 94158, USA.
Newhouse
Yvonne
Y
Hatters
Danny M
DM
Weisgraber
Karl H
KH
D015060:1,2-Dipalmitoylphosphatidylcholine / Q000737:chemistry*; D001057:Apolipoproteins E / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006801:Humans; D008024:Ligands; D050356:Lipid Metabolism; D008954:Models, Biological; D008958:Models, Molecular; D009991:Oscillometry; D011485:Protein Binding; D017433:Protein Structure, Secondary; D011973:Receptors, LDL / Q000737:chemistry / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry; D012542:Scattering, Radiation
D001057:Apolipoproteins E; D008024:Ligands; D011973:Receptors, LDL; D011994:Recombinant Proteins; D015060:1,2-Dipalmitoylphosphatidylcholine