A complete NMR spectral assignment of the lipid-free mouse apolipoprotein A-I (apoAI) C-terminal truncation mutant, apoAI(1-216) |
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| Authors: | Yunhuang Yang David Hoyt Jianjun Wang |
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| Institution: | (1) Department of Biochemistry and Molecular Biology, School of Medicine, Wayne State University, Detroit, MI 48201, USA;(2) High Field Magnetic Resonance Facility, EMSL, Pacific Northwest National Laboratory, Richland, WA 99352, USA |
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| Abstract: | ApoAI is the major protein component of the high-density lipoprotein (HDL) that has been a hot subject of interests because
of its anti-atherogenic properties. Lipid-free apoAI specifically binds to phospholipids, triggering HDL formation. Here we
report a complete backbone assignment and nearly complete sidechain assignment of a C-terminal 24-residue truncation mutant
of mouse apoAI, apoAI(1-216), in its lipid-free form. |
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| Keywords: | Apolipoprotein AI Atherosclerosis Reverse cholesterol transport HDL |
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