Crystallographic analysis of murine constitutive androstane receptor ligand-binding domain complexed with 5alpha-androst-16-en-3alpha-ol.
Crystallographic analysis of murine constitutive androstane receptor ligand-binding domain complexed with 5alpha-androst-16-en-3alpha-ol.
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与 5α-androst-16-en-3α-ol 复合的小鼠组成型雄甾烷受体配体结合域的晶体分析。
DOI：
10.1107/s1744309104032762
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发表时间：
2005
期刊：
影响因子：
--
通讯作者：
Fernandez,EliasJ
中科院分区：
文献类型：
--
作者：
Vincent,Jeremy;Shan,Li;Fan,Ming;Brunzelle,JosephS;Forman,BarryM;Fernandez,EliasJ
组成型雄烷受体（CAR）是核受体超家族的成员。与具有小分子配体诱导活性的经典核受体相反，CAR在明显不存在配体的情况下表现出组成型转录活性。CAR是最重要的转录因子之一，它协调调节微粒体细胞色素P450基因和其他药物代谢酶的表达。鼠CAR配体结合结构域（LBD）与类固醇受体共激活蛋白（SRC-1）受体相互作用结构域（RID）在大肠杆菌中共表达。通过亲和、阴离子交换和尺寸排阻色谱法从SRC-1中纯化mCAR LBD亚基，用雄烯醇结晶，并通过分子置换确定复合物的结构。
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.