RXR-like


Domain
zf-C4|RXR-like
Group
Zinc-Coordinating Group
PFAM
AnimalTFDB
Desciption
DNA-binding domain of retinoid X receptor (RXR) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. RXR functions as a DNA binding partner by forming heterodimers with other nuclear receptors including CAR, FXR, LXR, PPAR, PXR, RAR, TR, and VDR. All RXR heterodimers preferentially bind response elements composed of direct repeats of two AGGTCA sites with a 1-5 bp spacer. RXRs can play different roles in these heterodimers. RXR acts either as a structural component of the heterodimer complex, required for DNA binding but not acting as a receptor, or as both a structural and a functional component of the heterodimer, allowing 9-cis RA to signal through the corresponding heterodimer. In addition, RXR can also form homodimers, functioning as a receptor for 9-cis RA, independently of other nuclear receptors. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, RXR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD). [cite:PUB00121610], [cite:PUB00121611], [cite:PUB00121612], [cite:PUB00025660], [cite:PUB00121613], [cite:PUB00092048], [cite:PUB00092725], [cite:PUB00092726], [cite:PUB00016724], [cite:PUB00059514PMID:18971932
Rederence
  • Principles for modulation of the nuclear receptor superfamily. Gronemeyer H, Gustafsson JA, Laudet V. Nat Rev Drug Discov 3, 950-64, (2004).
  • Considerations on the structural evidence of a ligand-binding function of ultraspiracle, an insect homolog of vertebrate RXR. Jones G, Jones D. Insect Biochem Mol Biol 30, 671-9, (2000).
  • The retinoid X receptor and its ligands: versatile regulators of metabolic function, cell differentiation and cell death. Ahuja HS, Szanto A, Nagy L, Davies PJ. J Biol Regul Homeost Agents 17, 29-45, (2003).
  • The evolution of the nuclear receptor superfamily. Escriva H, Bertrand S, Laudet V. Essays Biochem. 40, 11-26, (2004).
  • RXR: from partnership to leadership in metabolic regulations. Desvergne B. Vitam Horm 75, 1-32, (2007).
  • International Union of Pharmacology. LXIII. Retinoid X receptors. Germain P, Chambon P, Eichele G, Evans RM, Lazar MA, Leid M, De Lera AR, Lotan R, Mangelsdorf DJ, Gronemeyer H. Pharmacol Rev 58, 760-72, (2006).
  • DNA recognition by nuclear receptors. Claessens F, Gewirth DT. Essays Biochem. 40, 59-72, (2004).
  • The structure of the ultraspiracle ligand-binding domain reveals a nuclear receptor locked in an inactive conformation. Clayton GM, Peak-Chew SY, Evans RM, Schwabe JW. Proc. Natl. Acad. Sci. U.S.A. 98, 1549-54, (2001).
  • Origins and evolutionary diversification of the nuclear receptor superfamily. Owen GI, Zelent A. Cell. Mol. Life Sci. 57, 809-27, (2000).
Statistic of Transcription Factors
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Transcription Factors Table

Statistic of Transcription Factors




Transcription Factor Table

Species

Gene ID Insect Gene Name Gene Symbol
iTF_00000389 Abrostola tripartita Atri006704.1 Hnf4
iTF_00000390 Abrostola tripartita Atri005895.1 NR2E3
iTF_00000391 Abrostola tripartita Atri010319.1 USP
iTF_00000392 Abrostola tripartita Atri021178.1 dsf
iTF_00000393 Abrostola tripartita Atri009406.1 svp
iTF_00000394 Abrostola tripartita Atri004304.1 nr2e1