Structure of the NF-kappa B p50 homodimer bound to DNA.
The structure of a large fragment of the p50 subunit of the human transcription factor NF-kappa B, bound as a homodimer to DNA, reveals that the Rel-homology region has two beta-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 carboxy-terminal dimerization domain bears the site of I-kappa B interaction. The folds of these domains are related to immunoglobulin-like modules. The amino-terminal domain also resembles the core domain of p53.
Howard Hughes Medical Institute, Cambridge, Massachusetts 02138.
C W
CW
Müller
F A
FA
Rey
M
M
Sodeoka
G L
GL
Verdine
S C
SC
Harrison
D000595:Amino Acid Sequence; D001483:Base Sequence; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D016328:NF-kappa B / Q000737:chemistry* / Q000378:metabolism; D052002:NF-kappa B p50 Subunit; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D011487:Protein Conformation; D011518:Proto-Oncogene Proteins / Q000737:chemistry; D020569:Proto-Oncogene Proteins c-rel; D011994:Recombinant Proteins / Q000737:chemistry
D016328:NF-kappa B; D052002:NF-kappa B p50 Subunit; D011518:Proto-Oncogene Proteins; D020569:Proto-Oncogene Proteins c-rel; D011994:Recombinant Proteins; D004247:DNA