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    FEBS Lett. 1995 Sep 4;371(2):199-203.

    Beta-sheet secondary structure of an LDL receptor domain from complement factor I by consensus structure predictions and spectroscopy.

    Ullman CG, Haris PI, Smith KF, Sim RB, Emery VC, Perkins SJ.

    Department of Biochemistry and Molecular Biology, University of Oxford, UK.

    Erratum in:

    • FEBS Lett 1996 Jan 29;379(2):201.

    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 beta-strands was predicted. Sequence threading against known protein folds indicated consistency with small beta-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 beta-sheet together with turns and loops. LDLr is proposed to have a beta-sheet structure in which the five biologically important Asp/Glu residues are located on an exposed loop.

    PMID: 7672128 [PubMed - indexed for MEDLINE]

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