Heteronuclear NMR studies of human serum apolipoprotein A‐I

FEBS Letters

Frank, Philippe G²  Cushley, Robert J¹  Okon, Mark¹  Marcel, Yves L² 

[1] Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, BC, Canada V5A 1S6;Lipoproteins and Atherosclerosis Research Group, University of Ottawa Heart Institute, Ottawa, ON, Canada K1Y 4E9

关键词: Protein structure;    Apolipoprotein;    Nuclear magnetic resonance;    Chemical shift index;    Torsion angle likelihood obtained from shift and sequence similarity;    Sodium dodecyl sulfate;    Apo;    apolipoprotein;    HDL;    high density lipoprotein;    SDS;    sodium dodecyl sulfate;    NMR;    nuclear magnetic resonance;    TOCSY;    total correlation spectroscopy;    NOESY;    nuclear Overhauser enhancement spectroscopy;    HSQC;    heteronuclear single quantum coherence;    CSI;    chemical shift index;    TALOS;    torsion angle likelihood obtained from shift and sequence similarity;   

DOI  :  10.1016/S0014-5793(02)02600-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The apolipoprotein A-I (apoA-I) solution structure in the presence of sodium dodecyl sulfate (SDS) was determined by combination of chemical shift index and torsion angle likelihood obtained from shift and sequence similarity methods. ApoA-I in lipid-mimetic solution is composed of α-helices (residues 8–32, 45–64, 67–77, 82–86, 90–97, 100–118, 122–140, 146–162, 167–205, 210–216 and 221–239), with 2–5 residue irregular segments between helical repeats, and the irregular segment 78–81 within helical repeat 2. ApoA-I is a monomer in the SDS complex and no evidence of interhelical interactions is found. Comparison of the apoA-I and apoA-I(1–186) [Okon et al., FEBS Lett. 487 (2001) 390–396] solution structures revealed that apoA-I undergoes a conformational change around Pro121.

【 授权许可】

Unknown