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β‐Sheet secondary structure of an LDL receptor domain from complement factor I by consensus structure predictions and spectroscopy
Author(s) -
Ullman Christopher G.,
Haris Parvez I.,
Smith Kathryn F.,
Sim Robert B.,
Emery Vincent C.,
Perkins Stephen J.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00916-w
Subject(s) - beta sheet , protein secondary structure , protein structure , receptor , chemistry , crystallography , peptide sequence , force spectroscopy , biophysics , biology , biochemistry , molecule , gene , organic chemistry
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.