A mutant form of ERα associated with estrogen insensitivity affects the coupling between ligand binding and coactivator recruitment

• DOI: 10.1126/scisignal.aaw4653
• Publication Date: 2020-09-22T23:15:56Z
• Authors: Yin Li; Laurel A. Coons; René Houtman; Kathryn E. Carlson; Teresa A. Martin; Christopher G. Mayne; Diana Melchers; Tanner B. Jefferson; J. Tyler Ramsey; John A. Katzenell...; Kenneth S. Korach
• Keywords: 0303 health sciences; Binding Sites; Drug Resistance; Estrogen Receptor alpha; Mutation, Missense; Estrogens; Hep G2 Cells; Molecular Dynamics Simulation; Ligands; Nuclear Receptor Coactivator 3; Kinetics; 03 medical and health sciences; HEK293 Cells; Nuclear Receptor Coactivator 1; Gene Expression Regulation; Protein Domains; Humans; Protein Binding

A patient-derived mutation in ERα that causes estrogen insensitivity alters coregulator recruitment.