Nuclear receptor
![Crystallographic structure of a heterodimer of the nuclear receptors PPAR-γ (green) and RXR-α (cyan) bound to double stranded DNA (magenta) and two molecules of the NCOA2 coactivator (red). The PPAR-γ antagonist GW9662 and RXR-α agonist retinoic acid are depicted as space-filling models (carbon = white, oxygen = red, nitrogen = blue, chlorine = green).[1]](/Images/godic/202501/24/PPARg_RXRa_3E002221.png")
![Structures of selected endogenous nuclear receptor ligands and the name of the receptor that each binds to.](/Images/godic/202501/24/NR_ligands2221.png")
![Structural Organization of Nuclear ReceptorsTop – Schematic 1D amino acid sequence of a nuclear receptor.Bottom – 3D structures of the DBD (bound to DNA) and LBD (bound to hormone) regions of the nuclear receptor. The structures shown are of the estrogen receptor. Experimental structures of N-terminal domain (A/B), hinge region (D), and C-terminal domain (F) have not been determined therefore are represented by red, purple, and orange dashed lines, respectively.](/Images/godic/202501/24/Nuclear_Receptor_Structure2221.png")
![](/Images/godic/202501/24/PR_DBD_2C7A2221.png")
In the field of molecular biology, nuclear receptors are a class of proteins found within cells that are responsible for sensing steroid and thyroid hormones and certain other molecules. In response, these receptors work with other proteins to regulate the expression of specific genes, thereby controlling the development, homeostasis, and metabolism of the organism.