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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, Vol. 60, No. Pt 6, 06.2004, p. 1170-2.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Pogenberg, V, Guichou, JF & Bourguet, W 2004, 'Purification and crystallization of the heterodimeric complex of RARbeta and RXRalpha ligand-binding domains in the active conformation', ACTA CRYSTALLOGR D, vol. 60, no. Pt 6, pp. 1170-2. https://doi.org/10.1107/S0907444904009928

APA

Pogenberg, V., Guichou, J. F., & Bourguet, W. (2004). Purification and crystallization of the heterodimeric complex of RARbeta and RXRalpha ligand-binding domains in the active conformation. ACTA CRYSTALLOGR D, 60(Pt 6), 1170-2. https://doi.org/10.1107/S0907444904009928

Vancouver

Pogenberg V, Guichou JF, Bourguet W. Purification and crystallization of the heterodimeric complex of RARbeta and RXRalpha ligand-binding domains in the active conformation. ACTA CRYSTALLOGR D. 2004 Jun;60(Pt 6):1170-2. https://doi.org/10.1107/S0907444904009928

Bibtex

@article{4cab694ca04c4667b03615320b594d68,
title = "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.",
keywords = "Alitretinoin, Animals, Dimerization, Escherichia coli/metabolism, Formates/chemistry, Genetic Vectors, Histidine/chemistry, Ligands, Mice, Protein Conformation, Protein Structure, Tertiary, Receptors, Retinoic Acid/chemistry, Retinoic Acid Receptor alpha, Tretinoin/chemistry, X-Ray Diffraction",
author = "Vivian Pogenberg and Guichou, {Jean Fran{\c c}ois} and William Bourguet",
note = "Copyright 2004 International Union of Crystallography",
year = "2004",
month = jun,
doi = "10.1107/S0907444904009928",
language = "English",
volume = "60",
pages = "1170--2",
journal = "ACTA CRYSTALLOGR D",
issn = "2059-7983",
publisher = "John Wiley and Sons Inc.",
number = "Pt 6",

}

RIS

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 -