Crystallization and preliminary X-ray analysis of the human androgen receptor ligand-binding domain with a coactivator-like peptide and selective androgen receptor modulators.
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.
Thauvin
Maxime
M
UMR 8015 CNRS, Université Paris Descartes, 4 Avenue de l'Observatoire, 75006 Paris, France.
Robin-Jagerschmidt
Catherine
C
Nique
François
F
Mollat
Patrick
P
Fleury
Damien
D
Prangé
Thierry
T
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
C410798:AR protein, human; D008024:Ligands; D010455:Peptides; D011944:Receptors, Androgen