title: Crystallization and preliminary X-ray analysis of the human androgen receptor ligand-binding domain with a coactivator-like peptide and selective androgen receptor modulators.
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(1)2(1)2(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.
authors.affiliation: UMR 8015 CNRS, Université Paris Descartes, 4 Avenue de l'Observatoire, 75006 Paris, France.
authors.forename: Maxime
authors.initials: M
authors.lastname: Thauvin
authors.forename: Catherine
authors.initials: C
authors.lastname: Robin-Jagerschmidt
authors.forename: François
authors.initials: F
authors.lastname: Nique
authors.forename: Patrick
authors.initials: P
authors.lastname: Mollat
authors.forename: Damien
authors.initials: D
authors.lastname: Fleury
authors.forename: Thierry
authors.initials: T
authors.lastname: Prangé
mesh_terms: D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D008024:Ligands; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011944:Receptors, Androgen / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism
chemical_list: C410798:AR protein, human; D008024:Ligands; D010455:Peptides; D011944:Receptors, Androgen