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

Publication ,  Journal Article
Zhou, XE; Suino-Powell, K; Ludidi, PL; McDonnell, DP; Xu, HE
Published in: Protein Expr Purif
May 2010

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.

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Published In

Protein Expr Purif

DOI

EISSN

1096-0279

Publication Date

May 2010

Volume

71

Issue

1

Start / End Page

21 / 27

Location

United States

Related Subject Headings

  • Trans-Activators
  • Sequence Alignment
  • Receptors, Androgen
  • Protein Structure, Tertiary
  • Protein Binding
  • Peptides
  • Molecular Sequence Data
  • Male
  • Humans
  • DNA
 

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Zhou, X. E., Suino-Powell, K., Ludidi, P. L., McDonnell, D. P., & Xu, H. E. (2010). Expression, purification and primary crystallographic study of human androgen receptor in complex with DNA and coactivator motifs. Protein Expr Purif, 71(1), 21–27. https://doi.org/10.1016/j.pep.2009.12.002
Zhou, X Edward, Kelly Suino-Powell, Phumzile L. Ludidi, Donald P. McDonnell, and H Eric Xu. “Expression, purification and primary crystallographic study of human androgen receptor in complex with DNA and coactivator motifs.Protein Expr Purif 71, no. 1 (May 2010): 21–27. https://doi.org/10.1016/j.pep.2009.12.002.
Zhou XE, Suino-Powell K, Ludidi PL, McDonnell DP, Xu HE. Expression, purification and primary crystallographic study of human androgen receptor in complex with DNA and coactivator motifs. Protein Expr Purif. 2010 May;71(1):21–7.
Zhou, X. Edward, et al. “Expression, purification and primary crystallographic study of human androgen receptor in complex with DNA and coactivator motifs.Protein Expr Purif, vol. 71, no. 1, May 2010, pp. 21–27. Pubmed, doi:10.1016/j.pep.2009.12.002.
Zhou XE, Suino-Powell K, Ludidi PL, McDonnell DP, Xu HE. Expression, purification and primary crystallographic study of human androgen receptor in complex with DNA and coactivator motifs. Protein Expr Purif. 2010 May;71(1):21–27.
Journal cover image

Published In

Protein Expr Purif

DOI

EISSN

1096-0279

Publication Date

May 2010

Volume

71

Issue

1

Start / End Page

21 / 27

Location

United States

Related Subject Headings

  • Trans-Activators
  • Sequence Alignment
  • Receptors, Androgen
  • Protein Structure, Tertiary
  • Protein Binding
  • Peptides
  • Molecular Sequence Data
  • Male
  • Humans
  • DNA