Nur77 (NR4A1) belongs to the NR4A family of orphan nuclear receptors. These nuclear receptors are essential in immune cell differentiation and metabolism, where they are involved in transcriptional control. Moreover, Nur77 over-expression is among the key factors driving T-cell exhaustion, which arises in many different cancers and diseases, highlighting the relevance of identifying its regulatory regions and defining potential inhibitors. Nur77 binds DNA through a highly conserved DNA binding domain (DBD), exerts its transcriptional activity via an unstructured N-terminal domain (NTD) and provides a potential ligand-binding interface via its ligand-binding domain (LBD). Previous efforts to identify inhibitors were focused exclusively on LBD, which proved to be largely unsuccessful, potentially due to the lack of canonical binding pocket in LBD. Here, we are focusing on NTD which is characterized by high levels of intrinsic disorder making it susceptible to phase separation. Due to this plasticity, NTD serves as an interaction hub for other proteins, making it a promising drug targeting region. We show how a peptide derived from a natural interaction partner of Nur77 reduces its transcriptional activity, via interaction with its N-terminal region. In addition, we are identifying intra and intermolecular interactions of Nur77 in order to understand its activity.