학술논문

Crystallization and preliminary X-ray analysis of the human androgen receptor ligand-binding domain with a coactivator-like peptide and selective androgen receptor modulators
Document Type
Academic Journal
Source
Acta Crystallographica Section F. Dec, 2008, Vol. 64 Issue 12, p1159, 4 p.
Subject
Peptides -- Analysis
Hormones, Sex -- Analysis
Language
English
ISSN
1744-3091
Abstract
To purchase or authenticate to the full-text of this article, please visit this link: http://dx.doi.org/10.1107/S1744309108036683 Byline: Maxime Thauvin, Catherine Robin-Jagerschmidt, Francois Nique, Patrick Mollat, Damien Fleury, Thierry Prange Keywords: androgen receptors; SARMs; coactivators Abstract: The ligand-binding domain of the human androgen receptor has been cloned, overproduced and crystallized in the presence of a coactivator-like 11-mer peptide and two different nonsteroidal ligands. The crystals of the two ternary complexes were isomorphous and belonged to space group P2.sub.12.sub.12.sub.1, with one molecule in the asymmetric unit. They diffracted to 1.7 and 1.95 A resolution, respectively. Structure determination of these two complexes will help in understanding the mode of binding of selective nonsteroidal androgens versus endogenous steroidal ligands and possibly the origin of their tissue selectivity. Author Affiliation: (a)UMR 8015 CNRS, Universite Paris Descartes, 4 Avenue de l'Observatoire, 75006 Paris, France (b)Proskelia, Parc Biocitech, 102 Avenue G. Roussel, 93230 Romainville, France Article History: Received 26 August 2008, accepted 7 November 2008 Article note: Thierry Prange, e-mail: thierry.prange@univ-paris5.fr