Crystallization and preliminary X-ray diffraction studies on the amino-terminal (receptor-binding) domain of human apolipoprotein E3 from serum very low density lipoproteins.
Human apolipoprotein E is a component of several classes of circulating plasma lipoproteins. In addition to binding lipids, this apolipoprotein, which is composed of two structural domains, mediates some lipoprotein-receptor interactions by binding to the low density lipoprotein receptor. The receptor-binding function, as well as some lipid-binding capability, is contained in the amino-terminal structural domain of apolipoprotein E. Thrombin-catalyzed hydrolysis of apolipoprotein E yields a fragment (residues 1 to 191) that has the same properties as, and seems to be a good model for, the amino-terminal domain. Crystals of this amino-terminal fragment suitable for high-resolution X-ray diffraction experiments have now been grown. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) and have unit cell dimensions of a = 86.0 A, b = 40.9 A, and c = 53.3 A (1 A = 0.1 nm). This is the first human serum apolipoprotein to be crystallized.
Aggerbeck
L P
LP
Centre de Génétique Moléculaire, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France.
Wetterau
J R
JR
Weisgraber
K H
KH
Mahley
R W
RW
Agard
D A
DA
D000595:Amino Acid Sequence; D053318:Apolipoprotein E3; D001057:Apolipoproteins E; D003460:Crystallization; D006801:Humans; D008079:Lipoproteins, VLDL / Q000032:analysis*; D014961:X-Ray Diffraction
D053318:Apolipoprotein E3; D001057:Apolipoproteins E; D008079:Lipoproteins, VLDL