S100P Interacts with p53 while Pentamidine Inhibits This Interaction.

ABSTRACT: S100P, a small calcium-binding protein, associates with the p53 protein with micromolar affinity. It has been hypothesized that the oncogenic function of S100P may involve binding-induced inactivation of p53. We used ¹H-¹⁵N HSQC experiments and molecular modeling to study the molecular interactions between S100P and p53 in the presence and absence of pentamidine. Our experimental analysis indicates that the S100P-53 complex formation is successfully disrupted by pentamidine, since S100P shares the same binding site for p53 and pentamidine. In addition, we showed that pentamidine treatment of ZR-75-1 breast cancer cells resulted in reduced proliferation and increased p53 and p21 protein levels, indicating that pentamidine is an effective antagonist that interferes with

SUBMITTER: Katte RH 

PROVIDER: S-EPMC8145327 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature