The decorin sequence SYIRIADTNIT binds collagen type I

被引:64
作者
Kalamajski, Sebastian
Aspberg, Anders
Oldberg, Ake [1 ]
机构
[1] Lund Univ, Dept Expt Med Sci, BMC B12, SE-22184 Lund, Sweden
[2] Univ Copenhagen, Dept Mol Biol, DK-2100 Copenhagen, Denmark
关键词
D O I
10.1074/jbc.M700073200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Decorin belongs to the small leucine-rich repeat proteoglycan family, interacts with fibrillar collagens, and regulates the assembly, structure, and biomechanical properties of connective tissues. The decorin-collagen type I-binding region is located in leucine-rich repeats 5-6. Site-directed mutagenesis of this 54-residue-long collagen-binding sequence identifies Arg-207 and Asp-210 in leucine-rich repeat 6 as crucial for the binding to collagen. The synthetic peptide SYIRIADTNIT, which includes Arg-207 and Asp-210, inhibits the binding of full-length recombinant decorin to collagen in vitro. These collagen-binding amino acids are exposed on the exterior of the beta-sheet-loop structure of the leucine-rich repeat. This resembles the location of interacting residues in other leucine-rich repeat proteins.
引用
收藏
页码:16062 / 16067
页数:6
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