Difference between revisions of "Nuclear receptors"
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|info=[http://www.ncbi.nlm.nih.gov/pubmed/22284354 Burris_2012_Chem Biol]; | |info=[http://www.ncbi.nlm.nih.gov/pubmed/22284354 Burris_2012_Chem Biol]; | ||
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In contrast to extracellular receptors such as the insulin receptor, intracellular receptors directely bind endocrine hormones and dietary lipids. Nuclear receptors interact directly with lipophilic ligands and bind to specific DNA response elements to regulate expression of target genes. All nuclear receptor members have a similar canonical domain structure that includes an N-terminal activation domain and conserved DNA and ligand-binding domains. | In contrast to extracellular receptors such as the insulin receptor, intracellular receptors directely bind endocrine hormones and dietary lipids. Nuclear receptors interact directly with lipophilic ligands and bind to specific DNA response elements to regulate expression of target genes. All nuclear receptor members have a similar canonical domain structure that includes an N-terminal activation domain and conserved DNA and ligand-binding domains. | ||
Well known members of the nuclear-receptor superfamily include the three different ligand-activated peroxisome proliverator activated receptor (PPAR) subtypes, PPAR-α, PPAR-β/δ, and PPAR-γ or the retinoid X receptor (RXR). | Well known members of the nuclear-receptor superfamily include the three different ligand-activated peroxisome proliverator activated receptor (PPAR) subtypes, [[PPAR-α]], [[PPAR-β/δ]], and [[PPAR-γ]] or the retinoid X receptor (RXR). |
Revision as of 16:36, 28 May 2012
Description
Nuclear receptors are ligand-dependent transcription factors.
Abbreviation: NRs
Reference: Burris_2012_Chem Biol;
In contrast to extracellular receptors such as the insulin receptor, intracellular receptors directely bind endocrine hormones and dietary lipids. Nuclear receptors interact directly with lipophilic ligands and bind to specific DNA response elements to regulate expression of target genes. All nuclear receptor members have a similar canonical domain structure that includes an N-terminal activation domain and conserved DNA and ligand-binding domains. Well known members of the nuclear-receptor superfamily include the three different ligand-activated peroxisome proliverator activated receptor (PPAR) subtypes, PPAR-α, PPAR-β/δ, and PPAR-γ or the retinoid X receptor (RXR).