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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), anadrol dbol stack. 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. The receptor has an N-terminal activation function-1 (AF-1) and a second activation function-2 (AF-2) in the C-terminal ligand-binding domain. The mechanisms of AF-1 and AF-2 gene activation, with emphasis on AF-1 and AF-2 conformation and co-activator binding, have been reviewed by Warnmark et al. The mechanism of AF-1 gene activation is not well understood due to the lack of conformational information but, by contrast, many crystal structures of the ligand-binding domain of different nuclear receptors have been achieved, allowing a fuller understanding of AF-2-mediated transcriptional activation. AF-2 is dependent on ligand binding to the receptor for its activity, which causes the folding of a C-terminal helix (helix-12), acting as a lid over the ligand pocket upon ligand binding. This folding creates the activation surface/AF-2 domain, allowing the docking of AF-2 co-activators and the formation of a charge clamp that stabilizes co-activator interaction, these co-activators having the leucine-X-X-leucine-leucine (LXXLL) motif necessary for such interaction (X is any amino acid). The molecular biology of the androgen receptor has been reviewed by Klocker et al. In contrast to other steroid receptors, most of its transcriptional activity is mediated through the N-terminal AF-1 domain, there being a reduced capacity of AF-2 in the androgen receptor to recruit LXXLL-containing co-activators. Instead, it has been suggested that the AF-2 of the androgen receptor acts primarily as an interaction platform for the recruitment of co-activators to the N-terminal region, this regulation of gene expression through the intradomain interaction and communication being unique to this receptor. To date, several families of co-activator proteins have been identified but only two direct inhibitors of androgen receptor function have been identified in vivo , SHP and DAX-1, these being atypical orphan receptors that lack DNA-binding domains. Using X-ray crystallography, the interaction between peptide segments of SHP containing LXXLL-like motifs and the ligand-binding domain on the androgen receptor was investigated, and it was found that the LKKIL motif formed a complex, binding with a hydrophobic groove on the androgen receptor (Jouravel et al. It was suggested that this transcriptional activity of androgen receptors might be inhibited by SHP competing for binding to androgen receptor co-activators. The binding motif to the androgen receptor by DAX-1 is still to be elucidated. Another corepressor, FoxG1, appears to be a likely candidate for interaction with the androgen receptor in vivo but studies are necessary to prove whether this is the case (Obendorf et al. Anabolic steroids bind to the androgen receptor with different affinities. The order of relative binding affinities in comparison with methyltrienolone, which had the strongest affinity, was nandrolone>methenolone>testosterone>mesterolone; a group which had relatively high and generally similar affinity for the androgen receptor in all three tissues. These investigators did not rank 17?-methyltestosterone, but it had a relative binding affinity of 0.
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