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
in 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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Protein Binding
/
Models, Molecular
/
NF-kappa B p50 Subunit
/
Protein Multimerization
Limits:
Humans
Language:
En
Journal:
Genes Dev
Journal subject:
BIOLOGIA MOLECULAR
Year:
2024
Document type:
Article
Affiliation country:
Estados Unidos
Country of publication:
Estados Unidos