Title : A mutant androgen receptor from patients with Reifenstein syndrome: identification of the function of a conserved alanine residue in the D box of steroid receptors.

Pub. Date : 1993 Dec

PMID : 8246999






7 Functional Relationships(s)
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1 A mutant androgen receptor from patients with Reifenstein syndrome: identification of the function of a conserved alanine residue in the D box of steroid receptors. Alanine androgen receptor Homo sapiens
2 Exchanging alanine 596 in the wild-type androgen receptor with serine or valine produced mutants with properties indistinguishable from those of the naturally occurring threonine 596 mutant receptor. Alanine androgen receptor Homo sapiens
3 These results indicate that an alanine residue at position 596 contributes important structural and functional activities to the androgen receptor. Alanine androgen receptor Homo sapiens
4 In the androgen receptor from the patients with Reifenstein syndrome, in which this alanine is converted to a threonine, wild-type receptor properties can be restored by exchanging an additional threonine at position 602 to an alanine. Alanine androgen receptor Homo sapiens
5 An alanine residue at position 596 or 602 in the DNA binding domain of the androgen receptor is therefore important for the full function of this receptor. Alanine androgen receptor Homo sapiens
6 In all steroid receptors that bind the core sequence AGAACANNNTGTTCT, an alanine residue is also present at a position equivalent to alanine 596 in the androgen receptor. Alanine androgen receptor Homo sapiens
7 In all steroid receptors that bind the core sequence AGAACANNNTGTTCT, an alanine residue is also present at a position equivalent to alanine 596 in the androgen receptor. Alanine androgen receptor Homo sapiens