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The DNA-binding domain targets the receptor to specific DNA sequences known as steroid (or hormone) response elements. On the receptor, the DNA-binding domain consists of two subdomains called ‘zinc-fingers’; each subdomain contains four cysteine residues that coordinate with a zinc atom, thus, stabilizing the ‘finger’ structure. The zinc-fingers are inserted between specific grooves of the DNA helix, thus, allowing maintenance of DNA-binding activity. A general model of steroid receptor action is displayed in Figure 7. In the absence of hormone, it is by and large accepted that steroid receptors exist as an inactive oligomeric complex, being sequestered by the heat-shock protein (Hsp), Hsp90, which acts as a molecular chaperone. Hsps are so-called because they were discovered to accumulate under stress conditions including within heat-traumatized cells, but many are present and functionally important under normal conditions; they are named according to their molecular weight in kilodaltons. Another chaperone called p23 stabilizes the aporeceptor complex by blocking Hsp90 in the ATP-bound substrate conformation. Co-chaperones utilizing tetratricopeptide repeat motifs are necessary for docking of the Hsp90. As an adjunct, other chaperones, called Hsp40 and Hsp70 and an organizing protein called Hop (heat-shock organizing protein) are important in the assembly of the steroid receptor’Hsp90 complex. Picard (2006) gives a clear overview of molecular chaperones and cofactors that are relevant to steroid receptor action, buy gp proviron 25 mg oral steroids $26.00 proviron. Phosphorylation of the receptors is also important in regulation of receptor function (Weigel and Moore, 2007). In the absence of hormone, the steroid receptor exists as an inactive oligomeric complex with the molecular chaperone heat-shock protein, Hsp90, and p23, and co-chaperones utilizing tetratricopeptide repeat (TPR) motifs. After hormone binding, the receptor’Hsp90 complex disassociates and the activated receptor is translocated into the nucleus. Activated receptors interact as homodimers with the steroid response element on the chromatin, triggering the formation of a transcription complex, a cluster of coregulators resulting in gene activation, transcription of the gene, protein translation, and a resultant alteration in cell function, growth or differentiation. This figure is redrawn in the own author’s style but was based on part of the figure in the article by Weigel and Moore (2007). The steroid receptor’Hsp90 complex appears to be necessary for the receptor to stabilize in a conformation for binding to the ligand with high affinity and also to maintain its solubility in the cell. It is generally accepted that, although the receptor is held in this complex, it is inactive as a transcription factor, that is, the Hsp90 complex acts as a repressor of transcriptional activity by preventing one or several of the following: nuclear localization, dimerization, DNA binding and interaction with transcriptional co-activators. Steroids are relatively small molecules, for example, testosterone has a molecular weight of 288, and they can passively diffuse into cells. In target tissues, that is, the cells that contain steroid receptors, the hormone binds to the receptor ligand-binding domain, causing dissociation of the receptor’Hsp90 complex, the resultant conformational (allosteric) change making the receptor active. In the case of the androgen (and glucocorticoid) receptor, the chaperone complex resides in the cytoplasm, and following dissociation from the chaperone the activated receptor is translocated into the nucleus. Activated receptors interact as homodimers with the steroid response element on the chromatin, the effect of two receptors binding being cooperative (greater affinity and stability). This attachment to the DNA, in turn, triggers the formation of a transcription complex, a cluster of coregulators (also called comodulators) that fit around the receptors like ‘pieces in a jigsaw puzzle’. Coregulators can be either positive or negative regulatory proteins, referred to as co-activators or corepressors, respectively (Perissi and Rosenfeld, 2005). Co-activator and corepressor complexes are required for nuclear receptor-mediated transcriptional regulation, generally liganded receptors recruiting co-activators resulting in gene activation, transcription of the gene, translation and a resultant alteration in cell function, growth or differentiation. The function of the transcriptional activation domains on the receptor is to mediate the binding of the receptor to the comodulators.
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