The thermodynamic influence of trapped water molecules on a protein-ligand interaction

Angew Chem Int Ed Engl. 2009;48(28):5207-10. doi: 10.1002/anie.200900481.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Cyclophilins / chemistry*
  • Cyclosporine / chemistry
  • Humans
  • Hydrogen Bonding
  • Ligands
  • Protein Structure, Tertiary
  • Thermodynamics
  • Water / chemistry*

Substances

  • Ligands
  • Water
  • Cyclosporine
  • Cyclophilins
  • PPIG protein, human