Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 275, Issue 29, Pages 21801-21804Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C000278200
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Funding
- NCI NIH HHS [R01 CA39481] Funding Source: Medline
- NHLBI NIH HHS [R01 HL63446] Funding Source: Medline
- NIAMS NIH HHS [R01 AR10481] Funding Source: Medline
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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 alpha 1(I) CB6 and is similar to 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.
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