The decorin sequence SYIRIADTNIT binds collagen type I.

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

The decorin sequence SYIRIADTNIT binds collagen type I. / Kalamajski, Sebastian; Aspberg, Anders; Oldberg, Ake.

In: Journal of Biological Chemistry, Vol. 282, No. 22, 2007, p. 16062-7.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Kalamajski, S, Aspberg, A & Oldberg, A 2007, 'The decorin sequence SYIRIADTNIT binds collagen type I.', Journal of Biological Chemistry, vol. 282, no. 22, pp. 16062-7. https://doi.org/10.1074/jbc.M700073200

APA

Kalamajski, S., Aspberg, A., & Oldberg, A. (2007). The decorin sequence SYIRIADTNIT binds collagen type I. Journal of Biological Chemistry, 282(22), 16062-7. https://doi.org/10.1074/jbc.M700073200

Vancouver

Kalamajski S, Aspberg A, Oldberg A. The decorin sequence SYIRIADTNIT binds collagen type I. Journal of Biological Chemistry. 2007;282(22):16062-7. https://doi.org/10.1074/jbc.M700073200

Author

Kalamajski, Sebastian ; Aspberg, Anders ; Oldberg, Ake. / The decorin sequence SYIRIADTNIT binds collagen type I. In: Journal of Biological Chemistry. 2007 ; Vol. 282, No. 22. pp. 16062-7.

Bibtex

@article{9d2ef15096d611dd86a6000ea68e967b,
title = "The decorin sequence SYIRIADTNIT binds collagen type I.",
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 = "Sebastian Kalamajski and Anders Aspberg and Ake Oldberg",
note = "Keywords: Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; Cattle; Collagen Type I; Extracellular Matrix Proteins; Mutagenesis, Site-Directed; Protein Binding; Proteoglycans; Recombinant Proteins",
year = "2007",
doi = "10.1074/jbc.M700073200",
language = "English",
volume = "282",
pages = "16062--7",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "22",

}

RIS

TY - JOUR

T1 - The decorin sequence SYIRIADTNIT binds collagen type I.

AU - Kalamajski, Sebastian

AU - Aspberg, Anders

AU - Oldberg, Ake

N1 - Keywords: Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; Cattle; Collagen Type I; Extracellular Matrix Proteins; Mutagenesis, Site-Directed; Protein Binding; Proteoglycans; Recombinant Proteins

PY - 2007

Y1 - 2007

N2 - 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.

AB - 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.

U2 - 10.1074/jbc.M700073200

DO - 10.1074/jbc.M700073200

M3 - Journal article

C2 - 17426031

VL - 282

SP - 16062

EP - 16067

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 22

ER -

ID: 6511497