A revisited version of the apo structure of the ligand-binding domain of the human nuclear receptor retinoic X receptor α.

ABSTRACT: The retinoic X receptor (RXR) plays a crucial role in the superfamily of nuclear receptors (NRs) by acting as an obligatory partner of several nuclear receptors; its role as a transcription factor is thus critical in many signalling pathways, such as metabolism, cell development, differentiation and cellular death. The first published structure of the apo ligand-binding domain (LBD) of RXRα, which is still used as a reference today, contained inaccuracies. In the present work, these inaccuracies were corrected using modern crystallographic tools. The most important correction concerns the presence of a π-bulge in helix H7, which was originally built as a regular α-helix. The presence of several CHAPS molecules, which are visible for the first time in the electron-density map and which stab

SUBMITTER: Eberhardt J 

PROVIDER: S-EPMC6360438 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature