Contribution of Electrostatic CH₃-π Interactions to Recognition of Histone Asymmetric Dimethylarginine by the SPIN1 Triple Tudor Domain.

ABSTRACT: Methylation of arginine (Arg) residues on histones creates a new binding epitope, enabling recognition by aromatic cage binding pockets in Tudor domains; these protein-protein interactions (PPIs) govern gene expression. Despite their biological importance, the molecular details of methylated Arg recognition are poorly understood. While the desolvation, hydrogen bonding, and guanidinium stacking of methylated Arg have been explored in model systems and proposed to contribute to binding, direct interactions between the methyl groups and the aromatic residues in the binding pocket have not previously been investigated. Herein, we mechanistically study the CH₃-π interactions between the SPIN1 triple Tudor domain and histone asymmetric dimethylarginine. We find that these CH₃

SUBMITTER: Travis CR 

PROVIDER: S-EPMC11407275 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature