[HTML][HTML] Interaction between the amino-and carboxyl-terminal regions of the rat androgen receptor modulates transcriptional activity and is influenced by nuclear …
T Ikonen, JJ Palvimo, OA Jänne - Journal of Biological Chemistry, 1997 - ASBMB
Identical N-terminal deletions in the wild-type rat androgen receptor (rAR) and a
constitutively active rAR (ARΔ641–902) devoid of the ligand-binding domain (LBD) resulted
in dissimilar consequences in transcriptional activation: deletion of residues 149–295
abolished wild-type AR activity, but did not influence that of ARΔ641–902. The activity of the
N-terminal transactivation domain is thus controlled by the hormone-occupied LBD,
suggesting that the N-and C-terminal regions of rAR communicate. Consistent with this idea …
constitutively active rAR (ARΔ641–902) devoid of the ligand-binding domain (LBD) resulted
in dissimilar consequences in transcriptional activation: deletion of residues 149–295
abolished wild-type AR activity, but did not influence that of ARΔ641–902. The activity of the
N-terminal transactivation domain is thus controlled by the hormone-occupied LBD,
suggesting that the N-and C-terminal regions of rAR communicate. Consistent with this idea …