The dimerization of the inhibitor of κB kinase subunit β (IKKβ) is required for its activation rather than its reactivity in the signalling of the nuclear factor-κB (NF-κB) pathway involved in inflammatory diseases. Molecular dynamics simulations were used to investigate how mutations and ligand binding affect dimerization of the protein assembly to probe the affinity for tyrosine and serine phosphorylation activation mechanisms. Intermolecular interactions, thermodynamic properties, and conformational changes were compared among the inactive, active, and null states of the kinase. Results suggest that the multimeric assembly mediates a global stability for the enzyme that influences the activity of IKKβ and highlights which activation mechanism is more favourable.

Selectivity in the activation mechanisms of inhibitor of κB kinase-β

2019 Spring National Meeting

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