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      Model structure of decorin and implications for collagen fibrillogenesis.

      The Journal of Biological Chemistry
      Amino Acid Sequence, Animals, Collagen, metabolism, Decorin, Enzyme Inhibitors, chemistry, Extracellular Matrix Proteins, Humans, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Proteins, Proteoglycans, Sequence Alignment

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          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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