Structure of the NF-κB p50 homodimer bound to DNA
Abstract
The structure of a large fragment of the p50 subunit of the human transcription factor NF-κB, bound as a homodimer to DNA, reveals that the Rel-homology region has two β-barrel domains that grip DNA in the major groove. Both domains contact the DNA backbone. The amino-terminal specificity domain contains a recognition loop that interacts with DNA bases; the car boxy-terminal dimerization domain bears the site of I-κB interaction. The folds of these domains are related to immunoglobulin-like modules. The amino-terminal domain also resembles the core domain of p53.
- Publication:
-
Nature
- Pub Date:
- January 1995
- DOI:
- 10.1038/373311a0
- Bibcode:
- 1995Natur.373..311M