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1: FEBS Lett. 1995 Sep 4;371(2):199-203.Click here to read Links
Erratum in:
FEBS Lett 1996 Jan 29;379(2):201.

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.

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]