title: Crystallization and preliminary X-ray diffraction studies on the amino-terminal (receptor-binding) domain of human apolipoprotein E3 from serum very low density lipoproteins.
abstract: 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.
authors.affiliation: Centre de Génétique Moléculaire, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France.
authors.forename: L P
authors.initials: LP
authors.lastname: Aggerbeck
authors.forename: J R
authors.initials: JR
authors.lastname: Wetterau
authors.forename: K H
authors.initials: KH
authors.lastname: Weisgraber
authors.forename: R W
authors.initials: RW
authors.lastname: Mahley
authors.forename: D A
authors.initials: DA
authors.lastname: Agard
mesh_terms: D000595:Amino Acid Sequence; D053318:Apolipoprotein E3; D001057:Apolipoproteins E; D003460:Crystallization; D006801:Humans; D008079:Lipoproteins, VLDL / Q000032:analysis*; D014961:X-Ray Diffraction
chemical_list: D053318:Apolipoprotein E3; D001057:Apolipoproteins E; D008079:Lipoproteins, VLDL