Title : Intermolecular NH2-/carboxyl-terminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity.

Pub. Date : 1998 Jan 2

PMID : 9417052






3 Functional Relationships(s)
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1 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. Steroids androgen receptor Homo sapiens
2 In a 2-hybrid protein interaction assay in mammalian cells, the steroid binding domain interacts with an NH2-terminal-DNA binding domain fragment and with the full-length androgen receptor at physiological androgen concentrations in a dose-dependent manner. Steroids androgen receptor Homo sapiens
3 The results suggest that steroid binding domain residues Val-889 and Arg-752 are critical to the NH2-/carboxyl-terminal interaction and that an intermolecular N-C interaction occurs during receptor dimerization that results in an antiparallel arrangement of androgen receptor monomers. Steroids androgen receptor Homo sapiens