RORs exhibit a domain structure that is typical of nuclear receptors and contain an N-terminal domain, a highly conserved DNA-binding domain (DBD) consisting of two C2-C2 zinc finger motifs, a ligand-binding domain (LBD), and a hinge domain spacing the DBD and LBD. The RORs regulate gene transcription by binding as monomers to ROR response elements (ROREs) consisting of the RGGTCA consensus preceded by an A/T-rich sequence in the regulatory regions of target genes. The ability to bind ROREs is shared with several other nuclear receptors, including the transcriptional repressors Rev-Erbα and Rev-Erbβ (NR1D1-2). By competing for RORE binding, these receptors can antagonize each other’s effects on transcription. For example, crosstalk between RORs and Rev-Erbs plays a role in the transcriptional regulation of a number of metabolic and clock genes.
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