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. 1996 Dec 13;271(50):31767-70.
doi: 10.1074/jbc.271.50.31767.

Model structure of decorin and implications for collagen fibrillogenesis

I T Weber  1 , R W Harrison, R V Iozzo
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Free article

Model structure of decorin and implications for collagen fibrillogenesis

I T Weber et al. J Biol Chem. .
Free article

Abstract

The three-dimensional structure of human decorin, a secreted proteoglycan involved in the regulation of collagen fibrillogenesis and cellular growth, has been modeled based on the crystal structure of the porcine ribonuclease inhibitor. Both proteins contain leucine-rich repeats and share 18% identical residues. This model structure of decorin has an arch shape with the single glycosaminoglycan chain and the three N-linked oligosaccharides located on the same side of the molecule. Decorin was modeled as binding to a polar sequence of collagen type I found in the d band. The inner concave surface is the appropriate size and shape to accommodate only one collagen triple helix of approximately 3 nm in length. The binding of one collagen triple helix to decorin is proposed to play a major role in the formation of the staggered arrangement of collagen molecules within the microfibrils by preventing lateral fusion of collagen molecules.

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