Meyer Sandra, Wang Ying-Hui, Pérez-Escrivà Pau, Kieffer Bruno
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.
Biomol NMR Assign. 2016 Apr;10(1):175-8. doi: 10.1007/s12104-015-9661-8. Epub 2016 Jan 5.
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.
雄激素受体（AR）属于核受体超家族，是依赖配体的转录因子。这种蛋白质与二氢睾酮等类固醇激素、特定DNA序列以及许多共调节因子结合。其中许多相互作用涉及N端结构域（NTD），预计该结构域具有内在无序性。为了提供有关AR NTD与其DNA结合结构域（DBD）之间可能的相互作用机制的功能信息，我们对人AR的一个片段进行了核磁共振研究，该片段包含NTD的最后37个残基和DBD（NTD-DBD518-627）。该片段的主链（1）H、（15）N、（13）C核磁共振共振归属表明AR NTD内存在残余螺旋二级结构。
