Published model of small-molecule binding and PR65 stabilization

Our paper was published in JACS Au

We are pleased to share our new publication in JACS Au, entitled: “Small Molecule Activators of Protein Phosphatase 2A Exert Global Stabilizing Effects on the Scaffold PR65.”

This collaborative study combines single-molecule optical tweezers, ensemble experiments, docking, and molecular dynamics simulations to investigate how small molecules affect PR65, the scaffold of protein phosphatase 2A. The results show that ATUX-8385 stabilizes the protein across its structure and reduces misfolding. The simulations help explain how ligand binding favors a conformation compatible with assembly of the PP2A complex.

Citation
Naqvi, M. M., Zacharopoulou, M., Saha, S., Banerjee, A., Yilmaz, S. Z., Sunderlikova, V., Johnson, C. M., Kumita, J. R., Yang, S. H., Gordon, R., Ohlmeyer, M., Tans, S. J., Gur, M., Bahar, I., Itzhaki, L. S. (2026). Small Molecule Activators of Protein Phosphatase 2A Exert Global Stabilizing Effects on the Scaffold PR65. JACS Au, 6(5), 2753-2765. (IF: 8.5; 5-year IF: 9.4)

View the publication
https://doi.org/10.1021/jacsau.6c00003

Published model of small-molecule binding and PR65 stabilization
Mechanistic model connecting small-molecule binding to PR65 conformation and PP2A assembly. Reproduced unchanged from Naqvi et al. (2026), Figure 8. Source