Structural and biochemical analyses of the nuclear IκBζ protein in complex with the NF-κB p50 homodimer.
Genes Dev
; 38(11-12): 528-535, 2024 Jul 19.
Article
em En
| MEDLINE
| ID: mdl-38960718
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 p50RelA heterodimers. Comparisons of IκBζp50 and p50κB DNA complex crystallographic models indicate that structural rearrangement is necessary for ternary complex formation of IκBζ and p50 with DNA.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ligação Proteica
/
Modelos Moleculares
/
Subunidade p50 de NF-kappa B
/
Multimerização Proteica
Limite:
Humans
Idioma:
En
Revista:
Genes Dev
Ano de publicação:
2024
Tipo de documento:
Article