Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site‐directed mutagenesis

FEBS Letters

Dahlbäck, Björn¹  Villoutreix, Bruno O.²  Duan, Jianxin³ 

[1] University of Lund, Department of Clinical Chemistry, Wallenberg Laboratory, University Hospital Malmö, S-205 02 Malmö, Sweden;INSERM U428, University of Paris V, School of Pharmacy, 4 Ave. de L'Observatoire, 75006 Paris, France;Center for Structural Biochemistry, Department of Biosciences at Novum, Karolinska Institute, S-141 57 Huddinge, Sweden

关键词: Apolipoprotein M;    Comparative modeling;    Lipocalin;    Site-directed mutagenesis;    ApoM;    apolipoprotein M;    MUP;    major urinary protein;    RBP;    retinol binding protein;    HDL;    high-density lipoprotein;   

DOI  :  10.1016/S0014-5793(01)02544-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein. Sensitive sequence searches, threading and comparative model building experiments revealed apoM to be structurally related to the lipocalin protein family. In a 3D model, characterized by an eight-stranded anti-parallel β-barrel, a segment including Asn135 could adopt a closed or open conformation. Using site-directed mutagenesis, we demonstrated Asn135 in wild-type apoM to be glycosylated, suggesting that the segment is solvent exposed. ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the β-barrel.

【 授权许可】

Unknown