Liver X receptor beta

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Nuclear receptor subfamily 1, group H, member 2
Protein NR1H2 PDB 1p8d.png
PDB rendering based on 1p8d.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols NR1H2 ; LXR-b; LXRB; NER; NER-I; RIP15; UNR
External IDs OMIM600380 MGI1352463 HomoloGene21397 IUPHAR: NR1H2 ChEMBL: 4093 GeneCards: NR1H2 Gene
RNA expression pattern
PBB GE NR1H2 218215 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 7376 22260
Ensembl ENSG00000131408 ENSMUSG00000060601
UniProt P55055 Q60644
RefSeq (mRNA) NM_001256647 NM_001285517
RefSeq (protein) NP_001243576 NP_001272446
Location (UCSC) Chr 19:
50.33 – 50.38 Mb
Chr 7:
44.55 – 44.55 Mb
PubMed search [1] [2]

Liver X receptor beta (LXR-β) is a member of the nuclear receptor family of transcription factors. LXR-β is encoded by the NR1H2 gene (nuclear receptor subfamily 1, group H, member 2).[1]

Function[edit]

The liver X receptors (LXRs) were originally identified as orphan members of the nuclear receptor superfamily because their ligands were unknown. Like other receptors in the family, LXRs heterodimerize with retinoid X receptor and bind to specific response elements (LXREs) characterized by direct repeats separated by 4 nucleotides. Two genes, alpha (LXRA) and beta, are known to encode LXR proteins.[1][2]

Structure[edit]

Crystal structure of human liver X receptor β(LXRβ) forming heterodimer with its' partner retinoid X receptor α(RXRα) on its cognate element , an AGGTCA direct repeat spaced by 4 nt shows an extended X-shaped arrangement, with DNA- and ligand-binding domains crossed. The LXRβ core binds DNA via canonical contacts and auxiliary DNA contacts that enhance affinity for the response element.[3]

Interactions[edit]

Liver X receptor beta has been shown to interact with NCOA6[4] and Retinoid X receptor alpha.[5]

References[edit]

  1. ^ a b "Entrez Gene: NR1H2 nuclear receptor subfamily 1, group H, member 2". 
  2. ^ Song C, Hiipakka RA, Kokontis JM, Liao S (June 1995). "Ubiquitous receptor: structures, immunocytochemical localization, and modulation of gene activation by receptors for retinoic acids and thyroid hormones". Ann. N. Y. Acad. Sci. 761: 38–49. doi:10.1111/j.1749-6632.1995.tb31367.x. PMID 7625741. 
  3. ^ Lou X., Toresson G., Benod C., Suh J. H., Philips K. J., Webb P.,Gustafsson JA (February 2014). "Structure of the retinoid X receptor α-liver X receptor β (RXRα-LXRβ) heterodimer on DNA". Nat. Struct. Mol. Biol. 21 (3): 277–281. doi:10.1038/nsmb.2778. PMID 24561505. 
  4. ^ Lee SK, Jung SY, Kim YS, Na SY, Lee YC, Lee JW (February 2001). "Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2". Mol. Endocrinol. 15 (2): 241–54. doi:10.1210/me.15.2.241. PMID 11158331. 
  5. ^ Seol W, Choi HS, Moore DD (January 1995). "Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors". Mol. Endocrinol. 9 (1): 72–85. doi:10.1210/mend.9.1.7760852. PMID 7760852. 

Further reading[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.