title: The thermodynamic influence of trapped water molecules on a protein-ligand interaction.
abstract: Water molecules doing time: Atomic-resolution crystal structures of the PPIase domain of cyclophilin G, alone and in complex with cyclosporin A, and together with MD simulations and calorimetry, reveal how trapped water molecules influence the thermodynamic profile of a protein-ligand interaction.
authors.affiliation: Research Group X-ray Crystallography, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
authors.forename: Christian M
authors.initials: CM
authors.lastname: Stegmann
authors.forename: Daniel
authors.initials: D
authors.lastname: Seeliger
authors.forename: George M
authors.initials: GM
authors.lastname: Sheldrick
authors.forename: Bert L
authors.initials: BL
authors.lastname: de Groot
authors.forename: Markus C
authors.initials: MC
authors.lastname: Wahl
mesh_terms: D018360:Crystallography, X-Ray; D021983:Cyclophilins / Q000737:chemistry*; D016572:Cyclosporine / Q000737:chemistry; D006801:Humans; D006860:Hydrogen Bonding; D008024:Ligands; D017434:Protein Structure, Tertiary; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*
chemical_list: D008024:Ligands; D014867:Water; D016572:Cyclosporine; D021983:Cyclophilins; C102923:PPIG protein, human