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Biochem Biophys Res Commun. 2000 Oct 14;277(1):209-15.

Molecular cloning and functional characterization of a novel nuclear receptor similar to an embryonic benzoate receptor BXR.

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Laboratory of Environmental Biochemistry, School of Pharmaceutical Sciences, Osaka University, 1-6 Yamada-oka, Suita, Osaka, 565, Japan.


Benzoate X receptor (BXR) is a member of the nuclear hormone receptor superfamily and is activated by alkyl esters of amino benzoic acids and expressed during early development stages. We report here a second BXR, which was cloned by screening Xenopus laevis embryonic cDNA libraries. This new BXR, termed BXRbeta, exhibits 97% identity in the DNA-binding domain and 79% identity in the ligand-binding domain in amino acid sequence to previously reported Xenopus BXR. The BXRbeta strongly binds as a heterodimer with retinoid X receptor (RXR) to direct repeats of an AGGTCA motif spaced 4 or 5 base pairs apart and activates transcription by addition of methyprednisolone and dexamethasone as well as amino- and hydroxybenzoates.

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