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Article

Glutamic acid 709 substitutions highlight the importance of the interaction between androgen receptor helices H3 and H12 for androgen and antiandrogen actions.

Molecular endocrinology (Baltimore, Md.) - 1 Apr 2006

Georget Virginie, Bourguet William, Lumbroso Serge, Makni Salouah, Sultan Charles, Nicolas Jean-Claude

Abstract excerpt

The mutation of a single amino acid in the ligand binding domain of the human androgen receptor (AR) can induce functional abnormalities; for example, in androgen binding or interactions with coregulators. We report here on the structure/function analysis of the ARE709K substitution that is associated with partial androgen insensitivity syndrome. We introduced several mutations at position 709 and tested the...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 16373394
DOI: 10.1210/me.2005-0419

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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