1xls
From Proteopedia
(New page: 200px<br /> <applet load="1xls" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xls, resolution 2.96Å" /> '''Crystal structure o...) |
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| - | [[Image:1xls.gif|left|200px]]<br /> | + | [[Image:1xls.gif|left|200px]]<br /><applet load="1xls" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1xls" size=" | + | |
caption="1xls, resolution 2.96Å" /> | caption="1xls, resolution 2.96Å" /> | ||
'''Crystal structure of the mouse CAR/RXR LBD heterodimer bound to TCPOBOP and 9cRA and a TIF2 peptide containg the third LXXLL motifs'''<br /> | '''Crystal structure of the mouse CAR/RXR LBD heterodimer bound to TCPOBOP and 9cRA and a TIF2 peptide containg the third LXXLL motifs'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Constitutive androstane receptor (CAR) induces xenobiotic, bilirubin, and | + | 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== | ==About this Structure== | ||
| - | 1XLS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with REA and TCD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1XLS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=REA:'>REA</scene> and <scene name='pdbligand=TCD:'>TCD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Cha, J | + | [[Category: Cha, J Y.]] |
| - | [[Category: Kliewer, S | + | [[Category: Kliewer, S A.]] |
[[Category: Li, Y.]] | [[Category: Li, Y.]] | ||
| - | [[Category: Repa, J | + | [[Category: Repa, J J.]] |
[[Category: Reynolds, R.]] | [[Category: Reynolds, R.]] | ||
[[Category: Suino, K.]] | [[Category: Suino, K.]] | ||
| - | [[Category: Xu, H | + | [[Category: Xu, H E.]] |
[[Category: peng, L.]] | [[Category: peng, L.]] | ||
[[Category: REA]] | [[Category: REA]] | ||
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[[Category: xenobiotic]] | [[Category: xenobiotic]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:56:21 2008'' |
Revision as of 13:56, 21 February 2008
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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 and 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 Thu Feb 21 15:56:21 2008
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
