Supporting information for Raman et al. (2003) Proc. Natl. Acad. Sci. USA, 10.1073/pnas.0437842100
Fig. 7.
Schematic representation of HSGAG–protein interaction. (Left) Representation of a HSGAG (purple) binding to a protein (red) with a constrained (narrow) binding surface (such as FGF-1 or -2) wherein the uniform helical structure of the HSGAG makes a sharp bend or kink to fit in the pocket. The sequence of the FGF-binding oligosaccharide is shown on the top with the trisaccharide spanning kink numbered from 1 to 3 and its location marked (white) in the HSGAG oligosaccharide. (Right) Representation of a HSGAG (purple) binding to a protein (green) with a wider binding surface (such as AT-III), thereby resulting in an overwind in the uniform helical structure to make maximum contact with the binding site on the protein. The sequence of the AT-III-binding pentasaccharide is shown on the top with the trisaccharide-spanning kink numbered from 1 to 3 and its location marked (white) in the HSGAG oligosaccharide. Note that in both representations the uniform helical structure continues after the kink, indicating that the kink is a local deviation induced on protein binding.