1OR2

APOLIPOPROTEIN E3 (APOE3) TRUNCATION MUTANT 165

1OR2 の概要

• エントリーDOI: 10.2210/pdb1or2/pdb
• 分子名称: APOLIPOPROTEIN E (2 entities in total)
• 機能のキーワード: lipid transport, heparin-binding, plasma protein, hdl, vldl, lipid binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted : P02649
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19485.39

構造登録者

Rupp, B.,Segelke, B.W.,Forstner, M. (登録日: 1999-03-25, 公開日: 2000-04-10, 最終更新日: 2024-10-30)

主引用文献

Segelke, B.W.,Forstner, M.,Knapp, M.,Trakhanov, S.D.,Parkin, S.,Newhouse, Y.M.,Bellamy, H.D.,Weisgraber, K.H.,Rupp, B.
Conformational flexibility in the apolipoprotein E amino-terminal domain structure determined from three new crystal forms: implications for lipid binding.
Protein Sci., 9:886-897, 2000

PubMed Abstract: An amino-terminal fragment of human apolipoprotein E3 (residues 1-165) has been expressed and crystallized in three different crystal forms under similar crystallization conditions. One crystal form has nearly identical cell dimensions to the previously reported orthorhombic (P2(1)2(1)2(1)) crystal form of the amino-terminal 22 kDa fragment of apolipoprotein E (residues 1-191). A second orthorhombic crystal form (P2(1)2(1)2(1) with cell dimensions differing from the first form) and a trigonal (P3(1)21) crystal form were also characterized. The structures of the first orthorhombic and the trigonal form were determined by seleno-methionine multiwavelength anomalous dispersion, and the structure of the second orthorhombic form was determined by molecular replacement using the structure from the trigonal form as a search model. A combination of modern experimental and computational techniques provided high-quality electron-density maps, which revealed new features of the apolipoprotein E structure, including an unambiguously traced loop connecting helices 2 and 3 in the four-helix bundle and a number of multiconformation side chains. The three crystal forms contain a common intermolecular, antiparallel packing arrangement. The electrostatic complimentarity observed in this antiparallel packing resembles the interaction of apolipoprotein E with the monoclonal antibody 2E8 and the low density lipoprotein receptor. Superposition of the model structures from all three crystal forms reveals flexibility and pronounced kinks in helices near one end of the four-helix bundle. This mobility at one end of the molecule provides new insights into the structural changes in apolipoprotein E that occur with lipid association.

PubMed: 10850798

実験手法

X-RAY DIFFRACTION (2.5 Å)