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Johs, A; Hammel, M; Waldner, I; May, RP; Laggner, P; Prassl, R.
Modular structure of solubilized human apolipoprotein B-100 - Low resolution model revealed by small angle neutron scattering
J Biol Chem. 2006; 281(28):19732-19739 Doi: 10.1074/jbc.M601688200 [OPEN ACCESS]
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Leading authors Med Uni Graz: Prassl Ruth
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Abstract:: 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.
Find related publications in this database (using NLM MeSH Indexing): Algorithms -; Apolipoprotein B-100 -; Apolipoproteins B - chemistry; Circular Dichroism -; Detergents - pharmacology; Humans -; Lipids - chemistry; Models, Molecular -; Models, Statistical -; Neutrons -; Protein Conformation -; Protein Structure, Secondary -; Scattering, Radiation -; Spectrophotometry -