Article
Heterodimeric complex of RAR and RXR nuclear receptor ligand-binding domains: purification, crystallization, and preliminary X-ray diffraction analysis.
Protein expression and purification - 1 Jul 2000
Bourguet W, Andry V, Iltis C, Klaholz B, Potier N, Van Dorsselaer A, Chambon P, Gronemeyer H, Moras D
Abstract excerpt
Both the human retinoic acid receptor alpha (hRARalpha) and a constitutively active mutant (F318A) of the mouse retinoid X receptor alpha (mRXR alpha F318A) ligand-binding domains were separately overexpressed in Escherichia coli, copurified as a heterodimer in a two-step procedure, and cocrystallized with an RAR alpha-specific antagonist by using polyethylene glycol 10,000 as precipitant. The crystals grew in...
Topics
- Animals
- Chromatography, Gel
- Crystallization
- Crystallography, X-Ray
- Escherichia coli
- Humans
- Ligands
- Mass Spectrometry
- Mice
- Mutation
- Protein Structure, Tertiary
- Receptors, Retinoic Acid
- Recombinant Proteins