Solvent Networks Tune Thermodynamics of Oligosaccharide Complex Formation in an Extended Protein Binding Site.The principles of protein-glycan binding are still not well understood on a molecular level.  Remarkably different thermodynamic binding signatures were found for different mutants; however, crystal structure analyses indicated that no major oligosaccharide or protein topology changes had occurred upon complex formation.  However, free energy calculations showed that a small water network inside the glucose-binding cavity had the most notable influence on the thermodynamic signature.  HK620TSP oligosaccharide binding shows that similar fundamental principles also apply for glycans, where a small number of water molecules can dominate the thermodynamic signature in an extended binding site.
THERM