1or2

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APOLIPOPROTEIN E3 (APOE3) TRUNCATION MUTANT 165

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known diseases associated with this structure: Alzheimer disease-2 OMIM:[107741], Hyperlipoproteinemia, type III OMIM:[107741], Macular degeneration, age-related OMIM:[107741], Myocardial infarction susceptibility OMIM:[107741], Sea-blue histiocyte disease OMIM:[107741]

About this Structure

1OR2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Conformational flexibility in the apolipoprotein E amino-terminal domain structure determined from three new crystal forms: implications for lipid binding., Segelke BW, Forstner M, Knapp M, Trakhanov SD, Parkin S, Newhouse YM, Bellamy HD, Weisgraber KH, Rupp B, Protein Sci. 2000 May;9(5):886-97. PMID:10850798

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