Purification and crystallization of the heterodimeric complex of RARbeta and RXRalpha ligand-binding domains in the active conformation
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Purification and crystallization of the heterodimeric complex of RARbeta and RXRalpha ligand-binding domains in the active conformation. / Pogenberg, Vivian; Guichou, Jean François; Bourguet, William.
in: ACTA CRYSTALLOGR D, Jahrgang 60, Nr. Pt 6, 06.2004, S. 1170-2.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Purification and crystallization of the heterodimeric complex of RARbeta and RXRalpha ligand-binding domains in the active conformation
AU - Pogenberg, Vivian
AU - Guichou, Jean François
AU - Bourguet, William
N1 - Copyright 2004 International Union of Crystallography
PY - 2004/6
Y1 - 2004/6
N2 - The ligand-binding domains of the retinoid X receptor alpha (RXRalpha) and of the retinoic acid receptor beta (RARbeta) were overexpressed separately and copurified in the heterodimeric form. Using a crystallization solution containing sodium formate and PEG 3350 as precipitant, the heterodimer was cocrystallized with the promiscuous ligand 9-cis-retinoic acid (9C-RA) and a 13-residue fragment of the nuclear receptor interaction domain (NID) of the transcriptional coactivator TRAP220. The crystals grew in the trigonal space group P3(1)21, with unit-cell parameters a = b = 115.7, c = 247.2 angstroms and two heterodimers per asymmetric unit. X-ray diffraction data were collected to 2.9 angstroms resolution. The structure was solved by molecular replacement and is currently being refined.
AB - The ligand-binding domains of the retinoid X receptor alpha (RXRalpha) and of the retinoic acid receptor beta (RARbeta) were overexpressed separately and copurified in the heterodimeric form. Using a crystallization solution containing sodium formate and PEG 3350 as precipitant, the heterodimer was cocrystallized with the promiscuous ligand 9-cis-retinoic acid (9C-RA) and a 13-residue fragment of the nuclear receptor interaction domain (NID) of the transcriptional coactivator TRAP220. The crystals grew in the trigonal space group P3(1)21, with unit-cell parameters a = b = 115.7, c = 247.2 angstroms and two heterodimers per asymmetric unit. X-ray diffraction data were collected to 2.9 angstroms resolution. The structure was solved by molecular replacement and is currently being refined.
KW - Alitretinoin
KW - Animals
KW - Dimerization
KW - Escherichia coli/metabolism
KW - Formates/chemistry
KW - Genetic Vectors
KW - Histidine/chemistry
KW - Ligands
KW - Mice
KW - Protein Conformation
KW - Protein Structure, Tertiary
KW - Receptors, Retinoic Acid/chemistry
KW - Retinoic Acid Receptor alpha
KW - Tretinoin/chemistry
KW - X-Ray Diffraction
U2 - 10.1107/S0907444904009928
DO - 10.1107/S0907444904009928
M3 - SCORING: Journal article
C2 - 15159591
VL - 60
SP - 1170
EP - 1172
JO - ACTA CRYSTALLOGR D
JF - ACTA CRYSTALLOGR D
SN - 2059-7983
IS - Pt 6
ER -