Decorin binds near the C terminus of type I collagen.
Decorin belongs to a family of small leucine-rich proteoglycans that are directly involved in the control of matrix organization and cell growth. Genetic evidence indicates that decorin is required for the proper assembly of collagenous matrices. Here, we sought to establish the precise binding site of decorin on type I collagen. Using rotary shadowing electron microscopy and photoaffinity labeling, we mapped the binding site of decorin protein core to a narrow region near the C terminus of type I collagen. This region is located within the cyanogen bromide peptide fragment alpha1(I) CB6 and is approximately 25 nm from the C terminus, in a zone that coincides with the c(1) band of the collagen fibril d-period. This location is very close to one of the major intermolecular cross-linking sites of collagen heterotrimers. Thus, decorin protein core possesses a unique binding specificity that could potentially regulate collagen fibril stability.
Keene
D R
DR
Shriners Hospital Research Facilities, Portland, Oregon 97201, USA.
San Antonio
J D
JD
Mayne
R
R
McQuillan
D J
DJ
Sarris
G
G
Santoro
S A
SA
Iozzo
R V
RV
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D058575:Decorin; D016326:Extracellular Matrix Proteins; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D011485:Protein Binding; D011509:Proteoglycans / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure
D058575:Decorin; D016326:Extracellular Matrix Proteins; D011509:Proteoglycans; D003094:Collagen