9LG0

Crystal Structure of Human Peroxiredoxin I in Complex with SAB

This is a non-PDB format compatible entry.

Summary for 9LG0

• Entry DOI: 10.2210/pdb9lg0/pdb
• Descriptor: Peroxiredoxin-1, Salvianolic Acid B (3 entities in total)
• Functional Keywords: dimer, oxidoreductase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 39394.76

Authors

Xu, H.,Luo, C. (deposition date: 2025-01-09, release date: 2025-10-01, Last modification date: 2025-11-19)

Primary citation

Dang, W.,Wang, X.,Li, H.,Xu, Y.,Li, X.,Huang, S.,Tao, H.,Li, X.,Yang, Y.,Xuan, L.,Xiao, W.,Guo, D.,Zhang, H.,Wu, Q.,Zheng, J.,Shen, X.,Chen, K.,Xu, H.,Zhang, Y.,Luo, C.
Augmentation of PRDX1-DOK3 interaction alleviates rheumatoid arthritis progression by suppressing plasma cell differentiation.
Acta Pharm Sin B, 15:3997-4013, 2025

PubMed Abstract: Rheumatoid arthritis (RA) is a chronic autoimmune disease characterized by persistent inflammation and joint damage, accompanied by the accumulation of plasma cells, which contributes to its pathogenesis. Understanding the genetic alterations occurring during plasma cell differentiation in RA can deepen our comprehension of its pathogenesis and guide the development of targeted therapeutic interventions. Here, our study elucidates the intricate molecular mechanisms underlying plasma cell differentiation by demonstrating that PRDX1 interacts with DOK3 and modulates its degradation by the autophagy-lysosome pathway. This interaction results in the inhibition of plasma cell differentiation, thereby alleviating the progression of collagen-induced arthritis. Additionally, our investigation identifies Salvianolic acid B (SAB) as a potent small molecular glue-like compound that enhances the interaction between PRDX1 and DOK3, consequently impeding the progression of collagen-induced arthritis by inhibiting plasma cell differentiation. Collectively, these findings underscore the therapeutic potential of developing chemical stabilizers for the PRDX1-DOK3 complex in suppressing plasma cell differentiation for RA treatment and establish a theoretical basis for targeting PRDX1-protein interactions as specific therapeutic targets in various diseases.

PubMed: 40893682
DOI: 10.1016/j.apsb.2025.06.006

Experimental method

X-RAY DIFFRACTION (1.81 Å)