Endocrine Abstracts

The mineralocorticoid receptor (MR) has a modular domain structure containing a C-terminal ligand-binding domain (LBD) that consists of 11 α-helices (designated H1 to H12) organized in an antiparallel helical sandwich. The LBD undergoes a conformational change upon aldosterone binding such that H12 forms a stable interaction with helices 3, 4 and 5 to create an AF-2 domain, a hydrophobic cleft on the surface of the LBD, which serves as a docking platform for transcription...