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Crystallographic analysis of murine constitutive androstane receptor ligand-binding domain complexed with

Jeremy Vincent1, Li Shan, Ming Fan

  • 1Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996, USA.

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
|March 2, 2006
PubMed

Insights

The constitutive androstane receptor (CAR) is a key transcription factor regulating drug metabolism. Researchers determined the crystal structure of the murine CAR ligand-binding domain complexed with androstenol.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • The constitutive androstane receptor (CAR) is a nuclear receptor superfamily member.
  • CAR displays constitutive transcriptional activity, unlike ligand-inducible receptors.
  • CAR regulates drug-metabolizing enzymes, including cytochrome P450s.

Purpose of the Study:

  • To elucidate the structural basis of CAR activity.
  • To determine the structure of the murine CAR ligand-binding domain (LBD) complexed with a ligand.

Main Methods:

  • Coexpression of murine CAR LBD and SRC-1 RID in E. coli.
  • Purification of mCAR LBD using affinity, anion-exchange, and size-exclusion chromatography.
  • Crystallization of the complex with androstenol and structure determination via molecular replacement.

Main Results:

  • Successfully purified the mCAR LBD subunit.
  • Determined the crystal structure of the mCAR LBD-androstenol complex.
  • Provided structural insights into CAR-coactivator interactions.

Conclusions:

  • The determined structure offers a foundation for understanding CAR regulation.
  • This structural information can aid in the development of novel therapeutics targeting CAR.

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