On the calculation of the binding force between decorin and collagen.

摘要

In the March 2005 issue of Journal of Biomechanics Vesentini et al. (2005) estimate theoretically the binding force between decorin and collagen using molecular modeling calculations. To derive the force constants of the interaction, the authors use a computer-generated structural model of a complex between one molecule of decorin core protein and one triple-helical collagen molecule. Although the methodology used in the study may be sound when applied to reliable, experimentally determined structures, we need to point out that the model used by the authors for the interaction between decorin and collagen is incorrect and therefore the conclusions extracted from the work are unlikely to be biologically relevant. We have recently determined the three-dimensional structure of the protein core of decorin by X-ray crystallography (Scott et al., 2004). This shows decorin to be an open arch-shaped structure that dimerizes through its concave surface. Previously, we had shown that decorin exists in solution as stable dimers, and had inferred from small-angle X-ray scattering studies the arrangement of monomers within these dimers that was subsequently seen in the crystal lattice (Scott et al., 2003).