Purification and crystallization of the heterodimeric complex of RARbeta and RXRalpha ligand-binding domains in the active conformation
Abstract
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.
Bibliografische Daten
Originalsprache | Englisch |
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ISSN | 0907-4449 |
DOIs | |
Status | Veröffentlicht - 06.2004 |
Extern publiziert | Ja |
Anmerkungen des Dekanats
Copyright 2004 International Union of Crystallography
PubMed | 15159591 |
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