Retinoid X receptor: Difference between revisions

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Michal Harel, Alexander Berchansky, Joel L. Sussman

Revision as of 15:35, 18 October 2012 view source Alexander Berchansky (talk \| contribs) 29,637 edits No edit summary ← Older edit		Revision as of 12:44, 14 November 2012 view source Michal Harel (talk \| contribs) 31,761 edits No edit summary Newer edit →
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	<StructureSection load='1g5y' size='400' side='right' caption='Structure of human retinoid X receptor ligand-binding domain complex with retinoid (PDB entry [[1g5y]])' scene=''>		<StructureSection load='1g5y' size='400' side='right' caption='Structure of human retinoid X receptor ligand-binding domain tetramer complex with retinoid (PDB entry [[1g5y]])' scene=''>

	'''Retinoid X receptor''' (RXR) is a nuclear receptor activated by 9-cis retinoic acid. RXR makes a heterodimer with subfamily 1 nuclear receptors including retinoic acid receptor (RAR). In the absence of ligand, the RAR/RXR complex binds the hormone response elements complexed with corepressor protein. Upon binding of the ligand, the corepressor disassociates from the receptor and associates with the coactivator leading to transcription activation. RAR contains a DNA-binding domain (DBD) and ligand-binding domain (LBD). There are 3 classes of RXR: α, β and γ.		'''Retinoid X receptor''' (RXR) is a nuclear receptor activated by 9-cis retinoic acid. RXR makes a heterodimer with subfamily 1 nuclear receptors including retinoic acid receptor (RAR). In the absence of ligand, the RAR/RXR complex binds the hormone response elements complexed with corepressor protein. Upon binding of the ligand, the corepressor disassociates from the receptor and associates with the coactivator leading to transcription activation. RAR contains a DNA-binding domain (DBD) and ligand-binding domain (LBD). There are 3 classes of RXR: α, β and γ.