{Reference Type}: Journal Article
{Title}: Structural and biochemical analyses of the nuclear IκBζ protein in complex with the NF-κB p50 homodimer.
{Author}: Zhu N;Rogers WE;Heidary DK;Huxford T;
{Journal}: Genes Dev
{Volume}: 38
{Issue}: 11
{Year}: 2024 Jul 19
{Factor}: 12.89
{DOI}: 10.1101/gad.351892.124
{Abstract}: As part of the efforts to understand nuclear IκB function in NF-κB-dependent gene expression, we report an X-ray crystal structure of the IκBζ ankyrin repeat domain in complex with the dimerization domain of the NF-κB p50 homodimer. IκBζ possesses an N-terminal α helix that conveys domain folding stability. Affinity and specificity of the complex depend on a small portion of p50 at the nuclear localization signal. The model suggests that only one p50 subunit supports binding with IκBζ, and biochemical experiments confirm that IκBζ associates with DNA-bound NF-κB p50:RelA heterodimers. Comparisons of IκBζ:p50 and p50:κB DNA complex crystallographic models indicate that structural rearrangement is necessary for ternary complex formation of IκBζ and p50 with DNA.