[HTML][HTML] Intermolecular NH2-/carboxyl-terminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity
E Langley, JA Kemppainen, EM Wilson - Journal of Biological Chemistry, 1998 - ASBMB
Structural alignment of the human androgen receptor dimer was investigated by introducing
steroid binding domain mutations that cause partial or complete androgen insensitivity into
fusion proteins containing the full-length androgen receptor or the steroid binding domain.
Most of the mutants had unchanged apparent equilibrium androgen binding affinity and
increased dissociation rates of [3 H] methyltrienolone and required increased
dihydrotestosterone concentrations for transcriptional activation. In a 2-hybrid protein …
steroid binding domain mutations that cause partial or complete androgen insensitivity into
fusion proteins containing the full-length androgen receptor or the steroid binding domain.
Most of the mutants had unchanged apparent equilibrium androgen binding affinity and
increased dissociation rates of [3 H] methyltrienolone and required increased
dihydrotestosterone concentrations for transcriptional activation. In a 2-hybrid protein …