PDBcal -- a comprehensive dataset for receptor-ligand interactions
What you can do:
A comprehensive dataset for receptor-ligand interactions with three-dimensional structures and binding thermodynamics from isothermal titration calorimetry.
Highlights:
- Compounds designed solely based on structure often do not result in any improvement of the binding affinity because of entropy-enthalpy compensation.
- Thermodynamic data along with structure provide an opportunity to gain a deeper understanding of this effect and aid in the refinement of scoring functions used in computational drug design.
- Here, we scoured the literature and constructed the most comprehensive hand-curated calorimetry dataset to date.
- It contains thermodynamic and structural data for more than 400 receptor-ligand complexes.
- The thermodynamic data consists of free energy, enthalpy, entropy and heat capacity as measured by isothermal titration calorimetry (ITC).
- The dataset also contains the experimental conditions that were used to carry out the ITC experiments.
- The chemical structures of the ligands are also provided.
Keywords:
- Calorimetry
- Drug Design
- Protein Binding
- Protein Conformation
- Thermodynamics
This record last updated: 08-13-2008