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. Author manuscript; available in PMC: 2021 Feb 2.
Published in final edited form as: Annu Rev Biochem. 2014 Mar 6;83:129–157. doi: 10.1146/annurev-biochem-060713-035314

Figure 3.

Figure 3

Heparan sulfate (HS) acts as a molecular scaffold. In all structures, proteins are shown in surface electrostatic potential, and the oligosaccharides are shown in stick representation. Each HS-binding site is enclosed in a dashed circle. (a) Cocrystal structure of thrombin, antithrombin (AT), and a hexadescasaccharide heparin mimic [Protein Data Bank (PDB) identifier 1TB6]. (b) Cocrystal structure of thrombin, protein C inhibitor (PCI), and a heparin-derived tetradecasaccharide. Because the tetradecasaccharide cannot be fully resolved in the cocrystal structure except for two sugar residues, it is manually modeled here (PDB 3B9F). (c) A model of the ternary complex of activated protein C (APC), PCI, and tetradecasaccharide based on PDB 3B9F and biochemical evidence (92). (d) Cocrystal structure of fibroblast growth factor 1 (FGF1), FGF receptor 2 (FGFR2, D2 and D3 domains), and heparin-derived decasaccharide (PDB 1E0O). (e) Cocrystal structure of FGF2, FGFR1 (D2 and D3 domains), and heparin-derived decasaccharide (PDB 1FQ9).