Inhibitor of KappaB Kinase (IKK) is a major regulation point on the NF-?B activation pathway. Recently we and other published crystal structures in three states of kinase activation; fully active, partially active, and inactive. These three structures reveal that the dimer unit of IKK gains increasing distance between the two kinase domains as it becomes active. This movement occurs within in the structural and dimerization domain(SDD). From this data we engineered a protein construct that stopped at this point. Here we investigate how this monomeric version of IKK compares to the the native dimeric, and how this can provide clues to the kinase's activation and specificity.

Monomeric IKK: Probing activation and specificty

248th National Meeting (2014)

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