Designing interactions by control of protein-ligand complex conformation : Tuning arginine-arene interaction geometry for enhanced electrostatic protein-ligand interactions
We investigated galectin-3 binding to 3-benzamido-2-O-sulfo-galactoside and -thiodigalactoside ligands using a combination of site-specific mutagenesis, X-ray crystallography, computational approaches, and binding thermodynamics measurements. The results reveal a conformational variability in a surface-exposed arginine (R144) side chain in response to different aromatic C3-substituents of bound ga