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 crystallographic structure of a homodimer of the NFKB1 protein (green and magenta) bound to DNA (brown).
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, 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]

References

^ ^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.
^ 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.
^ 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

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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): 311–7. doi:10.1038/373311a0. PMID 7830764.

[pmid9794820-2] 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.

[pmid15516339-3] 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.

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