1xls
From Proteopedia
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Crystal structure of the mouse CAR/RXR LBD heterodimer bound to TCPOBOP and 9cRA and a TIF2 peptide containg the third LXXLL motifs
Overview
Constitutive androstane receptor (CAR) induces xenobiotic, bilirubin, and, thyroid hormone metabolism as a heterodimer with the retinoid X receptor, (RXR). Unlike ligand-dependent nuclear receptors, CAR is constitutively, active. Here, we report the heterodimeric structure of the CAR and RXR, ligand binding domains (LBDs), which reveals an unusually large, dimerization interface and a small CAR ligand binding pocket. Constitutive, CAR activity appears to be mediated by the compact nature of the CAR LBD, that displays several unique features including a shortened AF2 helix and, helix H10, which are linked by a two-turn helix that normally adopts an, extended loop in other receptors, and an extended helix H2 that stabilizes, the canonical LBD fold by packing tightly against helix H3. These, structural observations provide a molecular framework for understanding, the atypical transcriptional activation properties of CAR.
About this Structure
1XLS is a Protein complex structure of sequences from Homo sapiens and Mus musculus with REA and TCD as ligands. Full crystallographic information is available from OCA.
Reference
The nuclear xenobiotic receptor CAR: structural determinants of constitutive activation and heterodimerization., Suino K, Peng L, Reynolds R, Li Y, Cha JY, Repa JJ, Kliewer SA, Xu HE, Mol Cell. 2004 Dec 22;16(6):893-905. PMID:15610733
Page seeded by OCA on Mon Nov 12 20:07:12 2007
Categories: Homo sapiens | Mus musculus | Protein complex | Cha, J.Y. | Kliewer, S.A. | Li, Y. | Repa, J.J. | Reynolds, R. | Suino, K. | Xu, H.E. | Peng, L. | REA | TCD | Car | Lbd | Nuclear receptor | Xenobiotic
