A three-dimensional homology model of lipid-free apolipoprotein A-IV using cross-linking and mass spectrometry.

ABSTRACT: Human apolipoprotein A-IV (apoA-IV) is a 46-kDa exchangeable plasma protein with many proposed functions. It is involved in chylomicron assembly and secretion, protection from atherosclerosis through a variety of mechanisms, and inhibition of food intake. There is little structural basis for these proposed functions due to the lack of a solved three-dimensional structure of the protein by x-ray crystallography or NMR. Based on previous studies, we hypothesized that lipid-free apoA-IV exists in a helical bundle, like other apolipoprotein family members and that regions near the N and C termini may interact. Utilizing a homobifunctional lysine cross-linking agent, we identified 21 intramolecular cross-links by mass spectrometry. These cross-links were used to constrain the building of a sequ

SUBMITTER: Tubb MR 

PROVIDER: S-EPMC2427326 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature