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The decorin sequence SYIRIADTNIT binds collagen type I.

Kalamajski, Sebastian LU ; Aspberg, Anders LU and Oldberg, Åke LU (2007) In Journal of Biological Chemistry 282(22). p.16062-16067
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
282
issue
22
pages
16062 - 16067
publisher
ASBMB
external identifiers
  • wos:000246794300014
  • scopus:34447536155
ISSN
1083-351X
DOI
10.1074/jbc.M700073200
language
English
LU publication?
yes
id
95618b0d-40c1-4d33-9e6c-48f82faba9cb (old id 167721)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17426031&dopt=Abstract
date added to LUP
2007-07-16 11:24:48
date last changed
2017-10-01 03:43:55
@article{95618b0d-40c1-4d33-9e6c-48f82faba9cb,
  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.},
  author       = {Kalamajski, Sebastian and Aspberg, Anders and Oldberg, Åke},
  issn         = {1083-351X},
  language     = {eng},
  number       = {22},
  pages        = {16062--16067},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {The decorin sequence SYIRIADTNIT binds collagen type I.},
  url          = {http://dx.doi.org/10.1074/jbc.M700073200},
  volume       = {282},
  year         = {2007},
}