Lipid-bound apoLp-III is less effective in binding to lipopolysaccharides and phosphatidylglycerol vesicles compared to the lipid-free protein
Author:
Funder
National Institutes of Health
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Clinical Biochemistry,Molecular Biology,General Medicine
Link
http://link.springer.com/content/pdf/10.1007/s11010-019-03530-x.pdf
Reference39 articles.
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2. Weise C, Franke P, Kopácek P, Wiesner A (1998) Primary structure of apolipophorin-III from the greater wax moth, Galleria mellonella. J Protein Chem 17:633–641
3. Wang J, Sykes BD, Ryan RO (2002) Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein. Proc Natl Acad Sci USA 99:1188–1193
4. Breiter DR, Kanost MR, Benning MM, Wesenberg G, Law JH, Wells MA, Rayment I, Holden HM (1991) Molecular structure of an apolipoprotein determined at 2.5 Å resolution. Biochemistry 30:603–608
5. Hård K, Van Doorn JM, Thomas-Oates JE, Kamerling JP, Van der Horst DJ (1993) Structure of the Asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate-linked 2-aminoethylphosphonate as a constituent of a glycoprotein. Biochemistry 32:766–775
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