The decorin sequence SYIRIADTNIT binds collagen type I.
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
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Journal | Journal of Biological Chemistry |
Volume | 282 |
Issue number | 22 |
Pages (from-to) | 16062-7 |
Number of pages | 5 |
ISSN | 0021-9258 |
DOIs | |
Publication status | Published - 2007 |
Bibliographical note
Keywords: Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; Cattle; Collagen Type I; Extracellular Matrix Proteins; Mutagenesis, Site-Directed; Protein Binding; Proteoglycans; Recombinant Proteins
ID: 6511497