The Rel homology domain (RHD) is a protein domain found in a family of eukaryotic transcription factors, which includes NF-κB, NFAT, among others. Some of these transcription factors appear to form multi-protein DNA-bound complexes.[2] Phosphorylation of the RHD appears to play a role in the regulation of some of these transcription factors, acting to modulate the expression of their target genes.[3] The RHD is composed of two immunoglobulin-like beta barrel subdomains that grip the DNA in the major groove. The N-terminal specificity domain resembles the core domain of the p53 transcription factor, and contains a recognition loop that interacts with DNA bases. The C-terminal dimerization domain contains the site for interaction with I-kappaB.[1]


  1. ^ a b PDB: 1SVC​;Müller CW, Rey FA, Sodeoka M, Verdine GL, Harrison SC (January 1995). "Structure of the NF-kappa B p50 homodimer bound to DNA". Nature. 373 (6512): 311–7. doi:10.1038/373311a0. PMID 7830764. 
  2. ^ Wolberger C (October 1998). "Combinatorial transcription factors". Curr. Opin. Genet. Dev. 8 (5): 552–9. doi:10.1016/S0959-437X(98)80010-5. PMID 9794820. 
  3. ^ Anrather J, Racchumi G, Iadecola C (January 2005). "cis-acting, element-specific transcriptional activity of differentially phosphorylated nuclear factor-kappa B". J. Biol. Chem. 280 (1): 244–52. doi:10.1074/jbc.M409344200. PMID 15516339. 

This article incorporates text from the public domain Pfam and InterPro IPR011539