9BOR

Structural and biochemical analyses of the nuclear I kappa B zeta protein in complex with the NF-kappa B p50 homodimer.

(2024) Genes Dev 38: 528-535

• PubMed: 38960718 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1101/gad.351892.124
• Primary Citation of Related Structures:  
  9BOR


• PubMed 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.

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Organizational Affiliation: 

Structural Biochemistry Laboratory, Department of Chemistry and Biochemistry, San Diego State University, San Diego, California 92182, USA.