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Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11

Kalamajski, Sebastian LU and Oldberg, Åke LU (2007) In Journal of Biological Chemistry 282(37). p.26740-26745
Abstract
Fibromodulin belongs to the small leucine-rich repeat proteoglycan family, interacts with collagen type I, and controls collagen fibrillogenesis and assembly. Here, we show that a major fibromodulin-binding site for collagen type I is located in leucine-rich repeat 11 in the C terminus of the leucine-rich repeat domain. We identified Glu-353 and Lys-355 in repeat 11 as essential for binding, and the synthetic peptide RLDGNEIKR, including Glu-353 and Lys-355, inhibits the binding of fibromodulin to collagen in vitro. Fibromodulin and lumican compete for the same binding region on collagen, and fibromodulin can inhibit the binding of lumican to collagen type I. However, the peptide RLDGNEIKR does not inhibit the binding of lumican to... (More)
Fibromodulin belongs to the small leucine-rich repeat proteoglycan family, interacts with collagen type I, and controls collagen fibrillogenesis and assembly. Here, we show that a major fibromodulin-binding site for collagen type I is located in leucine-rich repeat 11 in the C terminus of the leucine-rich repeat domain. We identified Glu-353 and Lys-355 in repeat 11 as essential for binding, and the synthetic peptide RLDGNEIKR, including Glu-353 and Lys-355, inhibits the binding of fibromodulin to collagen in vitro. Fibromodulin and lumican compete for the same binding region on collagen, and fibromodulin can inhibit the binding of lumican to collagen type I. However, the peptide RLDGNEIKR does not inhibit the binding of lumican to collagen, suggesting separate but closely situated fibromodulin- and lumican-binding sites in collagen. The collagen-binding Glu-353 and Lys-355 residues in fibromodulin are exposed on the exterior of the beta-sheet-loop structure of the leucine-rich repeat, which resembles the location of interacting residues in other leucine-rich repeat proteins, e. g. decorin. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Fibromodulin, collagen, Glu353, repeat 11, Lys355, type I, leucine-rich
in
Journal of Biological Chemistry
volume
282
issue
37
pages
26740 - 26745
publisher
ASBMB
external identifiers
  • wos:000249304900012
  • scopus:34848851981
ISSN
1083-351X
DOI
10.1074/jbc.M704026200
language
English
LU publication?
yes
id
5ef78189-ec01-47e8-9d1b-6801154bb647 (old id 657284)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17623650&dopt=Abstract
date added to LUP
2007-12-12 11:00:02
date last changed
2017-10-01 03:37:25
@article{5ef78189-ec01-47e8-9d1b-6801154bb647,
  abstract     = {Fibromodulin belongs to the small leucine-rich repeat proteoglycan family, interacts with collagen type I, and controls collagen fibrillogenesis and assembly. Here, we show that a major fibromodulin-binding site for collagen type I is located in leucine-rich repeat 11 in the C terminus of the leucine-rich repeat domain. We identified Glu-353 and Lys-355 in repeat 11 as essential for binding, and the synthetic peptide RLDGNEIKR, including Glu-353 and Lys-355, inhibits the binding of fibromodulin to collagen in vitro. Fibromodulin and lumican compete for the same binding region on collagen, and fibromodulin can inhibit the binding of lumican to collagen type I. However, the peptide RLDGNEIKR does not inhibit the binding of lumican to collagen, suggesting separate but closely situated fibromodulin- and lumican-binding sites in collagen. The collagen-binding Glu-353 and Lys-355 residues in fibromodulin are exposed on the exterior of the beta-sheet-loop structure of the leucine-rich repeat, which resembles the location of interacting residues in other leucine-rich repeat proteins, e. g. decorin.},
  author       = {Kalamajski, Sebastian and Oldberg, Åke},
  issn         = {1083-351X},
  keyword      = {Fibromodulin,collagen,Glu353,repeat 11,Lys355,type I,leucine-rich},
  language     = {eng},
  number       = {37},
  pages        = {26740--26745},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11},
  url          = {http://dx.doi.org/10.1074/jbc.M704026200},
  volume       = {282},
  year         = {2007},
}