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Steroid hormone receptors

Nuclear receptors Main article: nuclear receptor Steroid receptors of the nuclear receptor family are all transcription factors. Depending upon the type of receptor, they are either located in the cytosol and move to the cell nucleus upon activation, or remain in the nucleus waiting for the steroid hormone to enter and activate them. This uptake into the nucleus is facilitated by nuclear localization signal (NLS) found in the hinge region of the receptor. This region of the receptor is covered up by heat shock proteins (HSPs) which bind the receptor until the hormone is present. Upon binding by the hormone the receptor undergoes a conformational change releasing the HSP, and the receptor together with the bound hormone enter the nucleus to act upon transcription. Nuclear receptors Subfamily 3: Estrogen Receptor-like Group A: Estrogen receptor (Sex hormones: Estrogen) 1: Estrogen receptor-α (ERα; NR3A1, ESR1) 2: Estrogen receptor-β (ERβ; NR3A2, ESR2) Group C: 3-Ketosteroid receptors 1: Glucocorticoid receptor (GR; NR3C1) (Cortisol) 2: Mineralocorticoid receptor (MR; NR3C2) (Aldosterone) 3: Progesterone receptor (PR; NR3C3, PGR) (Sex hormones: Progesterone) 4: Androgen receptor (AR; NR3C4, AR) (Sex hormones: Testosterone) Structure Intracellular steroid hormone receptors share a common structure of four units that are functionally homologous, so-called "domains": Variable domain: It begins at the N-terminal and is the most variable domain between the different receptors. DNA binding domain: This centrally located highly conserved DNA binding domain (DBD) consists of two non-repetitive globular motifs[3] where zinc is coordinated with four cysteine and no histidine residues. Their secondary and tertiary structure is distinct from that of classic zinc fingers.[4] This region controls which gene will be activated. On DNA it interacts with the hormone response element (HRE). Hinge region: This area controls the movement of the receptor to the nucleus. Hormone binding domain: The moderately conserved ligand-binding domain (LBD) can include a nuclear localization signal, amino-acid sequences capable of binding chaperones and parts of dimerization interfaces. Such receptors are closely related to chaperones (namely heat shock proteins hsp90 and hsp56), which are required to maintain their inactive (but receptive) cytoplasmic conformation. At the end of this domain is the C-terminal. The terminal connects the molecule to its pair in the homodimer or heterodimer. It may affect the magnitude of the response. Mechanism of action Genomic Depending on their mechanism of action and subcellular distribution, nuclear receptors may be classified into at least two classes.[5][6] Nuclear receptors that bind steroid hormones are all classified as type I receptors. Only type I receptors have a heat shock protein (HSP) associated with the inactive receptor that will be released when the receptor interacts with the ligand. Type I receptors may be found in homodimer or heterodimer forms. Type II nuclear receptors have no HSP, and in contrast to the classical type I receptor are located in the cell nucleus. Free (that is, unbound) steroids enter the cell cytoplasm and interact with their receptor. In this process heat shock protein is dissociated, and the activated receptor-ligand complex is translocated into the nucleus. After binding to the ligand (steroid hormone), steroid receptors often form dimers. In the nucleus, the complex acts as a transcription factor, augmenting or suppressing transcription particular genes by its action on DNA. Type II receptors are located in the nucleus. Thus, their ligands pass through the cell membrane and cytoplasm and enter the nucleus where they activate the receptor without release of HSP. The activated receptor interacts with the hormone response element and the transcription process is initiated as with type I receptors. Non-genomic .