<i>In silico</i> characterization of the interaction of AKR1B1 with the deacetylase activation domain (DAD).

ABSTRACT: The aldo-keto reductase family 1 member B1 (AKR1B1) plays a key role in cancer progression by competing with histone deacetylase 3 to bind to the deacetylase activation domain (DAD) of the nuclear receptor corepressor SMRT. Previous studies showed that the L289A mutation in AKR1B1 disrupts its ability to form a dimer with DAD but further details of this interaction remain uncharacterized. This study aimed to model the DAD/AKR1B1 dimer by molecular docking and characterize the complex using molecular dynamics simulations. We identified a new model with increased structural stability for AKR1B1, reduced disruption of secondary structures of DAD, and lower ΔG than a previously reported one. In silico mutagenesis of AKR1B1 assessed the contributions from individual residues. We identifi

SUBMITTER: Gomez-Zaldivar FJ 

PROVIDER: S-EPMC12040874 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature