Thermodynamic Influence of Trapped Water Molecules on a Protein-Ligand Interaction

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.

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Bibliographische Detailangaben
Veröffentlicht in:	Angewandte Chemie (International ed.) 2009-01, Vol.48 (28), p.5207-5210
Hauptverfasser:	Stegmann, Christian M, Seeliger, Daniel, Sheldrick, George M, de Groot, Bert L, Wahl, Markus C
Format:	Artikel
Sprache:	eng
Schlagworte:	biophysics Crystallography, X-Ray Cyclophilins - chemistry Cyclosporine - chemistry drug design Humans Hydrogen Bonding isomerases Ligands molecular dynamics Protein Structure, Tertiary structural biology Thermodynamics Water - chemistry
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Beschreibung
Zusammenfassung:	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.
ISSN:	1433-7851 1521-3773
DOI:	10.1002/anie.200900481