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Fig. 5. (a) Turbidity vs. time curves for collagen alone (curve 1) and in the presence of 24 mg/ml recombinant (curve 2) or tissue-derived (curve 3) decorin. (b) Dependence of fibril growth rate (measured from the linear portions of turbidity vs. time curves) on the concentration of added tissue-derived decorin (open bars) or recombinant decorin (shaded bars). Data are shown as mean ± 1 SD (n = 2 or 3).

Fig. 6. Analysis of sedimentation equilibrium data by using Beckman XL-A/XL-I software, showing fit for single ideal species. The average molecular mass was calculated to be 147,700 ± 3,000 Da, which corresponds to dimeric decorin in solution.

Fig. 7. (a) Structural waters (cyan spheres) play a significant role in completing and extending hydrogen bonding networks between the two monomers. One pentagonal cluster of water molecules is trapped between the two molecules in the dimer (one monomer in green and the other monomer in red). Hydrogen bonds are shown as blue dotted lines. (b) Electrostatic charge distribution in the concave site of a decorin monomer (Upper) and glycoprotein Iba(Lower) (1, 2). There is no obvious clustering of charges in the decorin concave surface, but, rather, several charged residues that participate in dimer formation. Compare, for example, with the concave surface of glycoprotein Iba, which shows an obvious clustering of negative charges. That region corresponds to the known ligand-binding site for this protein (1, 2). (c) Surface representation of the decorin dimer colored by residue conservation in class I SLRPs. Two orthogonal views are shown, with conserved residues in yellow, partially conserved residues in green, and not conserved residues in gray. A noteworthy feature is a large contiguous patch of partially conserved residues (highlighted with a red circle in both views), which extends from the concave side of one monomer to the surface of the dimer free from N-linked glycosylation and involves leucine-rich repeats IV to VI (see main text).

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2. Uff, S., Clemetson, J. M., Harrison, T., Clemetson, K. J. & Emsley, J. (2002) J. Biol. Chem. 277, 35657-35663.