Expression, purification and primary crystallographic study of human androgen receptor in complex with DNA and coactivator motifs.

Published

Journal Article

The androgen receptor (AR) is a DNA-binding and hormone-activated transcription factor that plays critical roles in the development and progression of prostate cancer. The transcriptional function of AR is modulated by intermolecular interactions with DNA elements and coactivator proteins, as well as intramolecular interactions between AR domains; thus, the structural information from the full-length AR or a multi-domain fragment is essential for understanding the molecular basis of AR functions. Here we report the expression and purification of full-length AR protein and of a fragment containing its DNA-binding and ligand-binding domains connected by the hinge region in the presence of its natural ligand, dihydrotestosterone. Crystals of ligand-bound full-length AR and of the AR fragment in complex with DNA elements and coactivator motifs have been obtained and diffracted to low resolutions. These results help establish a foundation for pursuing further crystallographic studies of an AR/DNA complex.

Full Text

Duke Authors

Cited Authors

  • Zhou, XE; Suino-Powell, K; Ludidi, PL; McDonnell, DP; Xu, HE

Published Date

  • May 2010

Published In

Volume / Issue

  • 71 / 1

Start / End Page

  • 21 - 27

PubMed ID

  • 19995608

Pubmed Central ID

  • 19995608

Electronic International Standard Serial Number (EISSN)

  • 1096-0279

Digital Object Identifier (DOI)

  • 10.1016/j.pep.2009.12.002

Language

  • eng

Conference Location

  • United States