FEBS Letters | |
β‐Sheet secondary structure of an LDL receptor domain from complement factor I by consensus structure predictions and spectroscopy | |
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
【 预 览 】
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