The decorin sequence SYIRIADTNIT binds collagen type I.

Research output: Contribution to journalArticlepeer-review

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.
Original languageEnglish
Pages (from-to)16062-16067
JournalJournal of Biological Chemistry
Volume282
Issue number22
DOIs
Publication statusPublished - 2007

Subject classification (UKÄ)

  • Basic Medicine

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