Model structure of decorin and implications for collagen fibrillogenesis.
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.
Weber
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Department of Biochemistry and Molecular Pharmacology, Jefferson Medical College, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA. Iozzo@lac.jci.tju.edu
Harrison
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Iozzo
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D000595:Amino Acid Sequence; D000818:Animals; D003094:Collagen / Q000378:metabolism*; D058575:Decorin; D004791:Enzyme Inhibitors / Q000737:chemistry; D016326:Extracellular Matrix Proteins; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry; D011509:Proteoglycans / Q000737:chemistry*; D016415:Sequence Alignment
C546878:DCN protein, human; D058575:Decorin; D004791:Enzyme Inhibitors; D016326:Extracellular Matrix Proteins; D047908:Intracellular Signaling Peptides and Proteins; D011506:Proteins; D011509:Proteoglycans; C066953:ribonuclease inhibitor, porcine; D003094:Collagen