Public Data Set of Protein-Ligand Dissociation Kinetic Constants for Quantitative Structure-Kinetics Relationship Studies.

ABSTRACT: Protein-ligand binding affinity reflects the equilibrium thermodynamics of the protein-ligand binding process. Binding/unbinding kinetics is the other side of the coin. Computational models for interpreting the quantitative structure-kinetics relationship (QSKR) aim at predicting protein-ligand binding/unbinding kinetics based on protein structure, ligand structure, or their complex structure, which in principle can provide a more rational basis for structure-based drug design. Thus far, most of the public data sets used for deriving such QSKR models are rather limited in sample size and structural diversity. To tackle this problem, we have compiled a set of 680 protein-ligand complexes with experimental dissociation rate constants (k _off), which were mainly curated from

SUBMITTER: Liu H 

PROVIDER: S-EPMC9178723 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature