Backbone 1H, 15N, 13C NMR assignment of the 518-627 fragment of the androgen receptor encompassing N-terminal and DNA binding domains.
Fiche publication
Date publication
avril 2016
Journal
Biomolecular NMR assignments
Auteurs
Membres identifiés du Cancéropôle Est :
Dr KIEFFER Bruno
Tous les auteurs :
Meyer S, Wang YH, Pérez-Escrivà P, Kieffer B
Lien Pubmed
Résumé
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.
Mots clés
DNA, metabolism, Humans, Nuclear Magnetic Resonance, Biomolecular, Protein Domains, Protein Structure, Secondary, Receptors, Androgen, chemistry
Référence
Biomol NMR Assign. 2016 Apr;10(1):175-8