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Biomol NMR Assign. 2016 Apr;10(1):175-8. doi: 10.1007/s12104-015-9661-8. Epub 2016 Jan 5.

Backbone 1H, 15N, 13C NMR assignment of the 518-627 fragment of the androgen receptor encompassing N-terminal and DNA binding domains.

Author information

1
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.
2
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. kieffer@igbmc.fr.

Abstract

Androgen receptor (AR) belongs to the nuclear receptor superfamily that are ligand dependent transcription factors. This protein binds to steroid hormones such as dihydrotestosterone, to specific DNA sequences as well as to a number of co-regulatory factors. A number of these interactions involve the N-terminal domain (NTD), that is predicted to be intrinsically disordered. In order to provide functional information about possible cross-talk mechanisms between the AR NTD and its DNA binding domain (DBD), we have undertaken the NMR study of a fragment of human AR encompassing the last 37 residues of the NTD and the DBD (NTD-DBD518-627). The backbone (1)H, (15)N, (13)C NMR resonance assignments of this fragment indicate the presence of residual helical secondary structure within the AR NTD.

KEYWORDS:

Androgen receptor; DNA binding domain; Nuclear receptor

PMID:
26732902
DOI:
10.1007/s12104-015-9661-8
[Indexed for MEDLINE]

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