The N-terminal domain (NTD) and the ligand-binding domain (LBD) of the androgen receptor (AR) exhibit a ligand–dependent interaction (N/Cinteraction). Amino acids 3–36 in theNTD(AR3)36) play a dominant role in this interaction. Previously, it has been shown that a FxxFF motif inAR3)36 , 23 FxxLF 27 , is essential forLBDinteraction. We demonstrate in the current study that AR3)36 can be subdivided into two functionally distinct fragments: AR3)13 andAR16))13does not directly interact with the AR LBD, but rather contributes to the transactivation function of
