Research Paper Volume 13, Issue 18 pp 22544—22555

Glaucocalyxin B inhibits cartilage inflammatory injury in rheumatoid arthritis by regulating M1 polarization of synovial macrophages through NF-κB pathway

The targeted binding relationship between Gla B and P65. (A–C) 3D and 2D images of the binding between Gla B and P65. Gla B bound to the protein pocket of P65, and Gla B had hydrogen bond with Glu, Ser and Met. The binding energy was −8.4 kcal/mol, which could affect the phosphorylation and isomerization of P65. (D–F) Pull-down assay showed that Biotin-Gla B had a binding relationship with P65, and Gla B was an effective inhibitor of P65.

Figure 7. The targeted binding relationship between Gla B and P65. (AC) 3D and 2D images of the binding between Gla B and P65. Gla B bound to the protein pocket of P65, and Gla B had hydrogen bond with Glu, Ser and Met. The binding energy was −8.4 kcal/mol, which could affect the phosphorylation and isomerization of P65. (DF) Pull-down assay showed that Biotin-Gla B had a binding relationship with P65, and Gla B was an effective inhibitor of P65.