Cation-π interactions in protein-ligand binding: theory and data-mining reveal different roles for lysine and arginine.

ABSTRACT: We have studied the cation-π interactions of neutral aromatic ligands with the cationic amino acid residues arginine, histidine and lysine using ab initio calculations, symmetry adapted perturbation theory (SAPT), and a systematic meta-analysis of all available Protein Data Bank (PDB) X-ray structures. Quantum chemical potential energy surfaces (PES) for these interactions were obtained at the DLPNO-CCSD(T) level of theory and compared against the empirical distribution of 2012 unique protein-ligand cation-π interactions found in X-ray crystal structures. We created a workflow to extract these structures from the PDB, filtering by interaction type and residue pK_a. The gas phase cation-π interaction of lysine is the strongest by more than 10 kcal mol^-1, b

SUBMITTER: Kumar K 

PROVIDER: S-EPMC5903419 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature