Structure of NF-kappa B p50 homodimer bound to a kappa B site.
The 2.3-A crystal structure of the transcription factor NK-kappa B p50 homodimer bound to a palindromic kappa B site reveals that the Rel homology region folds into two distinct domains, similar to those in the immunoglobulin superfamily. The p50 dimer envelopes an undistorted B-DNA helix, making specific contacts along the 10-base-pair kappa B recognition site mainly through loops connecting secondary structure elements in both domains. The carboxy-terminal domains form a dimerization interface between beta-sheets using residues that are strongly conserved in the Rel family.
Ghosh
G
G
Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06510.
van Duyne
G
G
Ghosh
S
S
Sigler
P B
PB
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry*; D004330:Drosophila; D006801:Humans; D007136:Immunoglobulins / Q000737:chemistry; D051379:Mice; 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 / Q000378:metabolism; D020569:Proto-Oncogene Proteins c-rel; D012313:RNA; D017386:Sequence Homology, Amino Acid
D007136:Immunoglobulins; D016328:NF-kappa B; D052002:NF-kappa B p50 Subunit; D011518:Proto-Oncogene Proteins; D020569:Proto-Oncogene Proteins c-rel; D012313:RNA; D004247:DNA