Charged residues in the C-terminal domain of apolipoprotein A-I mediate oligomerization

Objectives: Apolipoprotein A-I (apoA-I) is an anti-atherogenic protein circulating in plasma, and is the major protein component of HDL. The N-terminal domain is made of a bundle of amphipathic α-helices, while the structure of the C-terminal (CT) domain is less defined. Lipid-free apoA-I exists as a heterogeneous population of oligomers, and the CT domain may be responsible for self-association. The objective of this study is to identify the residues in apoA-I responsible for oligomerization.