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 β-sheet-loop structure of the leucine-rich repeat. This resembles the location of interacting residues in other leucine-rich repeat proteins. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.
CITATION STYLE
Kalamajski, S., Aspberg, A., & Oldberg, Å. (2007). The decorin sequence SYIRIADTNIT binds collagen type I. Journal of Biological Chemistry, 282(22), 16062–16067. https://doi.org/10.1074/jbc.M700073200
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