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J Biol Chem, Vol. 274, Issue 45, 31755-31758, November 5, 1999
§¶,§,
From the Apolipoprotein A-I (apoA-I) is the principal
protein of high density lipoprotein particles (HDL). ApoA-I contains a
globular N-terminal domain (residues 1-43) and a lipid-binding
C-terminal domain (residues 44-243). Here we propose a detailed model
for the smallest discoidal HDL, consisting of two apoA-I molecules wrapped beltwise around a small patch of bilayer containing 160 lipid
molecules. The C-terminal domain of each monomer is ringlike, a curved,
planar amphipathic Department of Medicine, the
§ Atherosclerosis Research Unit, and the ¶ Department
of Biochemistry and Molecular Genetics, University of Alabama
Birmingham Medical Center, Birmingham, Alabama 35294
helix with an average of 3.67 residues per turn,
and with the hydrophobic surface curved toward the lipids. We have
explored all possible geometries for forming the dimer of stacked
rings, subject to the hypothesis that the optimal geometry will
maximize intermolecular salt bridge interactions. The resulting model
is an antiparallel arrangement with an alignment matching that of the
(nonplanar) crystal structure of lipid-free apoA-I.
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