The decorin sequence SYIRIADTNIT binds collagen type I.
Author
Summary, in English
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.
Department/s
- Åke Oldberg´s group
- Department of Experimental Medical Science
Publishing year
2007
Language
English
Pages
16062-16067
Publication/Series
Journal of Biological Chemistry
Volume
282
Issue
22
Links
Document type
Journal article
Publisher
American Society for Biochemistry and Molecular Biology
Topic
- Basic Medicine
Status
Published
Research group
- Åke Oldberg´s group
ISBN/ISSN/Other
- ISSN: 1083-351X