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Rel homology domain

Summary

The Rel homology domain (RHD) is a protein domain found in a family of eukaryotic transcription factors,[2] including both NF-κB and NFAT, among others. Some of these transcription factors appear to form multi-protein DNA-bound complexes.[3] 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.[4]

Rel homology domain (RHD)
Top view of the crystal structure of a homodimer of the Rel homology domains of NFKB1 (green and magenta) bound to DNA (orange).[1]
Identifiers
SymbolRHD
PfamPF00554
InterProIPR011539
PROSITEPDOC00924
SCOP21svc / SCOPe / SUPFAM
CDDcd07827
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1a02​, 1a3q​, 1a66​, 1bvo​, 1gji​, 1ikn​, 1imh​, le5​, le9​, 1lei​, 1nfa​,1nfi​, 1nfk​, 1ooa​, 1owr​, 1p7h​, 1pzu​, 1ram​, 1s9k​, 1svc​, 1uur​, 1uus​,1vkx​, 2as5​, 2ram​

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. In the case of NF-κB, the C-terminal dimerization subdomain determines dimerization propensity with other proteins in the NF-κB/Rel protein family. The dimerization subdomain is immediately followed by a nuclear localization sequence that also comprises the site for inhibitory interactions with IκB.[1]

References edit

  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): 311–317. doi:10.1038/373311a0. PMID 7830764. S2CID 4285677.
  2. ^ Biancalana M, Natan E, Lenardo MJ, Fersht AR (September 2021). "NF-κB Rel subunit exchange on a physiological timescale". Protein Science. 30 (9): 1818–1832. doi:10.1002/pro.4134. PMC 8376415. PMID 34089216.
  3. ^ Wolberger C (October 1998). "Combinatorial transcription factors". Current Opinion in Genetics & Development. 8 (5): 552–559. doi:10.1016/S0959-437X(98)80010-5. PMID 9794820.
  4. ^ Anrather J, Racchumi G, Iadecola C (January 2005). "cis-acting, element-specific transcriptional activity of differentially phosphorylated nuclear factor-kappa B". The Journal of Biological Chemistry. 280 (1): 244–252. doi:10.1074/jbc.M409344200. PMID 15516339.