Chemical shift assignments of the dimerization domain of NF-KappaB c-Rel subunit

The NF-κB family of transcription factors serve as master regulator of a broad range of cellular processes in vertebrates ranging from immune activation and inflammation to cell survival, proliferation, and development. The five NF-κB family members can potentially assemble into 15 different dimers, each capable of recognizing a 9-11 bp κB DNA sequence on its target-gene promoter/enhancer region. Here, we report the NMR backbone chemical shift assignment for the 23.2 kDa homodimer of NF-κB c-Rel subunit. In contrast to the ubiquitously expressed NF-κB subunits such as RelA and p50, c-Rel expression is confined largely to hematopoietic lineages. Dysregulated c-Rel activity drives immune dysfunction, chronic inflammation, and blood cancer. Chemical shift-derived secondary structure of the dimer is broadly consistent with existing DNA-bound crystal structures of the protein.