| Literature DB >> 17426031 |
Sebastian Kalamajski1, Anders Aspberg, Ake Oldberg.
Abstract
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.Entities:
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Year: 2007 PMID: 17426031 DOI: 10.1074/jbc.M700073200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157