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Rel homology domain

From Wikipedia, the free encyclopedia
Protein domain
Protein domain
Rel homology domain (RHD)
Top view of the crystal structure of a homodimer of the Rel homology domains ofNFKB1 (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

TheRel homology domain (RHD) is aprotein domain found in a family of eukaryotictranscription factors,[2] including bothNF-κB andNFAT, among others. Some of these transcription factors appear to form multi-proteinDNA-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 twoimmunoglobulin-likebeta barrel subdomains that grip the DNA in the major groove. TheN-terminal specificity domain resembles the core domain of thep53 transcription factor, and contains a recognition loop that interacts with DNA bases. In the case ofNF-κB, theC-terminal dimerization subdomain determines dimerization propensity with other proteins in theNF-κB/Rel protein family. The dimerization subdomain is immediately followed by anuclear localization sequence that also comprises the site for inhibitory interactions withIκB.[1]

References

[edit]
  1. ^abPDB: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.Bibcode:1995Natur.373..311M.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.
This article incorporates text from the public domainPfam andInterPro:IPR011539
(1) Basic domains
(1.1) Basicleucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3)bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2)Zinc finger DNA-binding domains
(2.1)Nuclear receptor(Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3.1)Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3)Fork head /winged helix
(3.4)Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4)β-Scaffold factors with minor groove contacts
(4.1)Rel homology region
(4.2)STAT
(4.3) p53-like
(4.4)MADS box
(4.6)TATA-binding proteins
(4.7)High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3)Pocket domain
(0.5)AP-2/EREBP-related factors
(0.6) Miscellaneous
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