Open AccessCrystallographic analysis of murine constitutive androstane receptor ligand‐binding domain complexed with 5α‐androst‐16‐en‐3α‐ol
Author(s) -
Vincent Jeremy,
Shan Li,
Fan Ming,
Brunzelle Joseph S.,
Forman Barry M.,
Fernandez Elias J.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309104032762
Subject(s) - constitutive androstane receptor , nuclear receptor , steroid , coactivator , androstane , receptor , nuclear receptor coactivator 1 , ligand (biochemistry) , chemistry , estrogen related receptor gamma , protein subunit , cytochrome p450 , biochemistry , transcription factor , biology , microbiology and biotechnology , gene , stereochemistry , enzyme , hormone
The constitutive androstane receptor (CAR) is a member of the nuclear receptor superfamily. In contrast to classical nuclear receptors, which possess small‐molecule ligand‐inducible activity, CAR exhibits constitutive transcriptional activity in the apparent absence of ligand. CAR is among the most important transcription factors; it coordinately regulates the expression of microsomal cytochrome P450 genes and other drug‐metabolizing enzymes. The murine CAR ligand‐binding domain (LBD) was coexpressed with the steroid receptor coactivator protein (SRC‐1) receptor‐interacting domain (RID) in Escherichia coli . The mCAR LBD subunit was purified away from SRC‐1 by affinity, anion‐exchange and size‐exclusion chromatography, crystallized with androstenol and the structure of the complex determined by molecular replacement.