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Chembiochem. 2014 Nov 3;15(16):2370-3. doi: 10.1002/cbic.201402420. Epub 2014 Sep 11.

Reversible amyloid fiber formation in the N terminus of androgen receptor.

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Institut de Génétique et de Biologie Moléculaire et Cellulaire, INSERM, U596, CNRS, UMR-7104, Université de Strasbourg, 1 rue Laurent Fries, 67404 Illkirch-Graffenstaden (France); NMRTEC S.A.S. Boulevard Sébastien Brandt, Bioparc, Bât. B, 67400 Illkirch-Graffenstaden (France).


Most of the biological effects of androgen hormones are mediated through an intracellular transcription factor, the androgen receptor (AR). This protein presents a long disordered N-terminal domain (NTD), known to aggregates into amyloid fibers.1 This aggregation property is usually associated with the presence of a poly-glutamine tract (polyQ), known to be involved in several pathologies.2 The NTD has gain interest recently because potential anti-prostate-cancer molecules could target this domain.3 Here, we characterize a conserved region of the NTD (distal from polyQ); it promotes the formation of amyloid fibers under mild oxidative conditions. Unlike most fibrils, which are irreversibly aggregated, the free peptides can be restored from the fibril by the addition of a reducing agent.


amyloid beta-peptides; androgen receptor; dimerization; disulfide bridge; self-assembly

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