Structural and biochemical analyses of the nuclear IκBζ protein in complex with the NF-κB p50 homodimer (in EN)
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.
- Research Organization:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States). Advanced Light Source (ALS)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC02-05CH11231
- OSTI ID:
- 2582470
- Journal Information:
- Genes & Development, Journal Name: Genes & Development Journal Issue: 11-12 Vol. 38; ISSN 0890-9369
- Publisher:
- Cold Springs Harbor Laboratory Press
- Country of Publication:
- United States
- Language:
- EN
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