The dimerization of the inhibitor of κB kinase subunit β (IKKβ) is required for its activation rather than its reactivity in the signaling of the nuclear factor-κB (NF-κB) pathway involved in inflammatory diseases. Molecular dynamics simulations were used to investigate the protein-protein and protein-ligand interactions associated with activation of IKKβ. Intermolecular interactions, conformational changes, and binding free energies were compared between a monomer and two dimers and suggest that there is selectivity in the activation of IKKβ.

Structure-activity and conformational-activity relationships of inhibitor of κB kinase-β

249th National Meeting (2015)

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