Androgen receptor: Difference between revisions

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DBD is a cysteine-rich region that is the most highly conserved in the steroid hormone nuclear receptor family <ref name="Structure" />, but it has been shown that binding of selective androgen response elements (AREs) allow the specific activation functions of the AR. They facilitate direct DNA binding of the AR to the promoter and enhancer regions of AR-regulated genes, thereby allowing the activation functions of the N-terminal and LBD to stimulate or repress the transcription of these genes <ref name="Bench to Bedside" />.

AR ~~is a~~ dimer, like other steroid receptors, ~~consisting~~ of two equal, common hexameric half-sites, separated by a 3 base-pair spacer <ref name="Structure" />. This domain is critical for AR function, due to its role in dimerization and binding of dimerized AR to select motifs on target DNA <ref name="AR" />.

AR dimer structure, like other steroid receptors, consists of two equal, common hexameric half-sites, separated by a 3 base-pair spacer <ref name="Structure" />. This domain is critical for AR function, due to its role in dimerization and binding of dimerized AR to select motifs on target DNA <ref name="AR" />.

Each DBD monomer has a core composed of two zinc finger motifs, which consists of four cysteine residues that coordinate a zinc ion <ref name="Structure" />. The first one is closer to the NTD which has the P box, identical in all the family, that controls the DNA binding specificity at AREs <ref name="AR" />. The second zinc finger motif facilitates AR dimerization via the D box.

Androgen receptor: Difference between revisions

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@@ Line 14: / Line 14: @@
 DBD is a cysteine-rich region that is the most highly conserved in the steroid hormone nuclear receptor family <ref name="Structure" />, but it has been shown that binding of selective androgen response elements (AREs) allow the specific activation functions of the AR. They facilitate direct DNA binding of the AR to the promoter and enhancer regions of AR-regulated genes, thereby allowing the activation functions of the N-terminal and LBD to stimulate or repress the transcription of these genes <ref name="Bench to Bedside" />.
-AR is a dimer, like other steroid receptors, consisting of two equal, common hexameric half-sites, separated by a 3 base-pair spacer <ref name="Structure" />. This domain is critical for AR function, due to its role in dimerization and binding of dimerized AR to select motifs on target DNA <ref name="AR" />.
+AR dimer structure, like other steroid receptors, consists of two equal, common hexameric half-sites, separated by a 3 base-pair spacer <ref name="Structure" />. This domain is critical for AR function, due to its role in dimerization and binding of dimerized AR to select motifs on target DNA <ref name="AR" />.
 Each DBD monomer has a core composed of two zinc finger motifs, which consists of four cysteine residues that coordinate a zinc ion <ref name="Structure" />. The first one is closer to the NTD which has the P box, identical in all the family, that controls the DNA binding specificity at AREs <ref name="AR" />. The second zinc finger motif facilitates AR dimerization via the D box.