Apolipophorin III (apoLp-III) is an insect-derived exchangeable apolipoprotein. The structure of lipid-free apoLp-III is an up-and-down helix bundle consisting of five helices connected by short loops. A high-resolution structure of the physiologically active, lipid-bound form of apoLp-III is not available to date. The lipid-bound apoLp-III is proposed to adapt an antiparallel, fully extended conformation, which surrounds the periphery of the lipid-bilayer in discoidal lipid-protein complexes. This study aims to gain insight into the structure of lipid-bound apoLp-III by proteolysis with trypsin, chymotrypsin, endoproteinase Glu-C and elastase. All four proteases completely cleaved lipid-free apoLp-III. In apoLp-III · dimyristoylphosphatidylcholine nanodiscs, lipid-bound apoLp-III was protected by phospholipids and not susceptible to the proteases, except for endoproteinase Glu-C. In lipid-bound apoLp-III, E63, E126 and E137 were cleaved by endoproteinase Glu-C. The results indicate that these residues are exposed to the solvent in lipid-bound apoLp-III in nanodiscs.
|Advisor:||Weers, Paul M. N.|
|School:||California State University, Long Beach|
|School Location:||United States -- California|
|Source:||MAI 51/05M(E), Masters Abstracts International|
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