β‐Sheet secondary structure of an LDL receptor domain from complement factor I by consensus structure predictions and spectroscopy

FEBS Letters

Ullman, Christopher G.²  Sim, Robert B.¹  Haris, Parvez I.²  Perkins, Stephen J.²  Emery, Vincent C.³  Smith, Kathryn F.² 

[1] MRC Immunochemistry Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK;Department of Biochemistry and Molecular Biology, University of Oxford, South Parks Road, Oxford OX1 3QU, UK;Department of Virology, Royal Free Hospital School of Medicine, Rowland Hill Street, London NW3 2PF, UK

关键词: LDLr domain;    FT-IR spectroscopy;    Secondary structure prediction;    Protein fold recognition;    β-Sheet protein;    LDLr2;    second low density lipoprotein receptor domain of factor I;    FT-IR;    Fourier transform infrared;    CD;    circular dichroism;    NMR;    nuclear magnetic resonance;   

DOI  :  10.1016/0014-5793(95)00916-W

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Low density lipoprotein receptor domains (LDLrs) represent a large cell surface receptor superfamily of consensus length 39 residues. Alignment of 194 sequences indicated highly conserved Cys and Asp/Glu residues, and a consensus secondary structure with three β-strands was predicted. Sequence threading against known protein folds indicated consistency with small β-sheet proteins. Complement factor I contains two LDLrs, and the second of these was successfully expressed using a bacterial pGEX system. FT-IR spectroscopy on this indicated a small amount of β-sheet together with turns and loops. LDLr is proposed to have a β-sheet structure in which the five biologically important Asp/Glu residues are located on an exposed loop.

【 授权许可】

Unknown