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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/167721
- author
- Kalamajski, Sebastian
LU
; Aspberg, Anders
LU
and Oldberg, Åke
LU
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 282
- issue
- 22
- pages
- 16062 - 16067
- publisher
- American Society for Biochemistry and Molecular Biology
- 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
- 2016-04-01 11:56:36
- date last changed
- 2022-04-21 00:03:39
@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 = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{The decorin sequence SYIRIADTNIT binds collagen type I.}},
url = {{http://dx.doi.org/10.1074/jbc.M700073200}},
doi = {{10.1074/jbc.M700073200}},
volume = {{282}},
year = {{2007}},
}