Rel homology domain

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1a02, 1a3q, 1a66, 1bvo, 1gji, 1ikn, 1imh, le5, le9, 1lei, 1nfa,1nfi, 1nfk, 1ooa, 1owr, 1p7h, 1pzu, 1ram, 1s9k, 1svc, 1uur, 1uus,1vkx, 2as5, 2ram

Rel homology domain (RHD)
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
Symbol	RHD
Pfam	PF00554
InterPro	IPR011539
PROSITE	PDOC00924
SCOP2	1svc / SCOPe / SUPFAM
CDD	cd07827
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1a02, 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 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]

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

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.
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.
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.
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.

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

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[pmid7830764-1] 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.

[pmid9794820-3] 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.

[pmid15516339-4] 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.