title: Binding free energy calculations of galectin-3-ligand interactions.
abstract: Galectins show remarkable binding specificity towards beta-galactosides. A recently developed method for calculating binding free energies between a protein and its substrates has been used to evaluate the binding specificity of galectin-3. Five disaccharides and a tetrasaccharide were used as the substrates. The calculated binding free energies agree quite well with the experimental data and the ranking of binding affinities is well reproduced. For all the six protein-ligand complexes it was observed that electrostatic interactions oppose binding whereas the non-polar contributions drive complex formation. The observed binding specificity of galectin-3 for galactosides rather than glucosides is discussed in light of our results.
authors.affiliation: Department of Chemistry, University of Calcutta, 92 APC Road, Kolkata-700 009, India.
authors.forename: Tarun K
authors.initials: TK
authors.lastname: Mandal
authors.forename: Chaitali
authors.initials: C
authors.lastname: Mukhopadhyay
mesh_terms: D002236:Carbohydrate Conformation; D003198:Computer Simulation; D004187:Disaccharides / Q000378:metabolism; D037502:Galectin 3 / Q000737:chemistry* / Q000378:metabolism*; D006860:Hydrogen Bonding; D008024:Ligands; D008956:Models, Chemical; D008958:Models, Molecular; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D055672:Static Electricity; D013379:Substrate Specificity; D013816:Thermodynamics
chemical_list: D004187:Disaccharides; D037502:Galectin 3; D008024:Ligands; D011134:Polysaccharides