A detailed molecular belt model for apolipoprotein A-I in discoidal high density lipoprotein.
作者： Jere P. Segrest , Martin K. Jones , Anthony E. Klon , Christopher J. Sheldahl , Matthew Hellinger
关键词: Dimer 、 Bilayer 、 Protein structure 、 Monomer 、 Crystallography 、 Molecule 、 Intermolecular force 、 Chemistry 、 Crystal structure 、 Antiparallel (biochemistry)
摘要: 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 lipid-binding C-terminal 44–243). Here we propose detailed model for smallest discoidal HDL, consisting two apoA-I molecules wrapped beltwise around small patch bilayer containing 160 lipid molecules. The each monomer ringlike, curved, planar amphipathic α helix with an average 3.67 residues per turn, hydrophobic surface curved toward lipids. We have explored all possible geometries forming dimer stacked rings, subject to hypothesis that optimal geometry will maximize intermolecular salt bridge interactions. resulting antiparallel arrangement alignment matching (nonplanar) crystal structure lipid-free apoA-I.
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