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Sebastian Kalamajski

Assistant researcher

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The decorin sequence SYIRIADTNIT binds collagen type I.

Author

  • Sebastian Kalamajski
  • Anders Aspberg
  • Åke Oldberg

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

Document type

Journal article

Publisher

ASBMB

Topic

  • Basic Medicine

Status

Published

Research group

  • Åke Oldberg´s group

ISBN/ISSN/Other

  • ISSN: 1083-351X