<p>Computational and experimental evidence supporting activation of the FABP5–NF-κB signaling axis.</p>

(D) RMSD profiles from MD simulations showing that the FABP5–IκBα and FABP5–P65 complexes reached equilibrium after ~80 ns, whereas the FABP5–IKKβ complex exhibited reduced stability. (E) Rg analysis demonstrating stable global compactness of the FABP5–IκBα, FABP5-IKKβ and FABP5–P65 complexes during MD simulations.

(F) SASA analysis showing mild fluctuations for the FABP5–IκBα and FABP5-IKKβ complex and minimal variation for the FABP5–P65 complex. (G) Hydrogen bond analysis illustrating persistent intermolecular hydrogen bonding between FABP5 and NF-κB pathway proteins, with a higher average number observed in the FABP5–P65 complex. (H) RMSF analysis indicating limited residue-level flexibility and high structural stability of the FABP5–IκBα and FABP5–P65 complexes.