Journal
PROTEIN EXPRESSION AND PURIFICATION
Volume 71, Issue 1, Pages 21-27Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2009.12.002
Keywords
Androgen receptor; Crystallization; Ligand-binding domain; DNA-binding domain; Androgen response elements
Categories
Funding
- Michigan Economic Development Corporation
- Michigan Technology Tri-Corridor [085PI 000817]
- Office of Science of the U.S. Department of Energy
- Jay and Betty Van Andel Foundation
- National Institutes of Health [DK071662, DK066202, HL089301]
- Department of Defense Prostate Cancer [W81XWH0510043]
- U.S. Department of Defense (DOD) [W81XWH0510043] Funding Source: U.S. Department of Defense (DOD)
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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. (C) 2009 Elsevier Inc. All rights reserved.
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