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J. Biol. Chem., Vol. 281, Issue 28, 19732-19739, July 14, 2006

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Modular Structure of Solubilized Human Apolipoprotein B-100

LOW RESOLUTION MODEL REVEALED BY SMALL ANGLE NEUTRON SCATTERING^*

Alexander Johs, Michal Hammel, Ines Waldner, Roland P. May^¶, Peter Laggner, and Ruth Prassl¹

From the Institute of Biophysics and X-ray Structure Research, Austrian Academy of Sciences, Schmiedlstrasse 6, A-8042 Graz, Austria, the Division of Cell Biology and Biophysics, School of Biological Sciences, University of Missouri, Kansas City, Missouri 64110, and the ^¶Institut Laue-Langevin, 6, rue Jules Horowitz, BP 156, 38042 Grenoble Cedex 9, France

Being intimately involved in cholesterol transport and lipid metabolism human low density lipoprotein (LDL) plays a prominent role in atherogenesis and cardiovascular diseases. The receptor-mediated cellular uptake of LDL is triggered by apolipoprotein B-100 (apoB-100), which represents the single protein moiety of LDL. Due to the size and hydrophobic nature of apoB-100, its structure is not well characterized. Here we present a low resolution structure of solubilized apoB-100. We have used small angle neutron scattering in combination with advanced shape reconstruction algorithms to generate a three-dimensional model of lipid-free apoB-100. Our model clearly reveals that apoB-100 is composed of distinct domains connected by flexible regions. The apoB-100 molecule adopts a curved shape with a central cavity. In comparison to LDL-associated apoB-100, the lipid-free protein is expanded, whereas according to spectroscopic data the secondary structure is widely preserved. Finally, the low resolution model was used as a template to reconstruct a hypothetical domain organization of apoB-100 on LDL, including information derived from a secondary structure prediction.

Received for publication, February 22, 2006 , and in revised form, April 28, 2006.

^* This work was supported by the Austrian Science Fund (P16479). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement"in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

This article was selected as a Paper of the Week.

¹ To whom correspondence should be addressed. Tel.: 43-316-4120-305; Fax: 43-316-4120-390; E-mail: ruth.prassl{at}oeaw.ac.at.

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