Aromatic interactions at the ligand-protein interface: Implications for the development of docking scoring functions.

ABSTRACT: The ability to design and fine-tune non-covalent interactions between organic ligands and proteins is indispensable to rational drug development. Aromatic stacking has long been recognized as one of the key constituents of ligand-protein interfaces. In this communication, we employ a two-parameter geometric model to conduct a large-scale statistical analysis of aromatic contacts in the experimental and computer-generated structures of ligand-protein complexes, considering various combinations of aromatic amino acid residues and ligand rings. The geometry of interfacial π-π stacking in crystal structures accords with experimental and theoretical data collected for simple systems, such as the benzene dimer. Many contemporary ligand docking programs implicitly treat aromatic stacking with van

SUBMITTER: Brylinski M 

PROVIDER: S-EPMC5818208 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature