1xls

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[[Image:1xls.gif|left|200px]]<br /><applet load="1xls" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1xls.gif|left|200px]]
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caption="1xls, resolution 2.96&Aring;" />
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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'''<br />
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{{Structure
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|PDB= 1xls |SIZE=350|CAPTION= <scene name='initialview01'>1xls</scene>, resolution 2.96&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=REA:RETINOIC+ACID'>REA</scene> and <scene name='pdbligand=TCD:3,5-DICHLORO-2-{4-[(3,5-DICHLOROPYRIDIN-2-YL)OXY]PHENOXY}PYRIDINE'>TCD</scene>
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|ACTIVITY=
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|GENE= human ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), mouse ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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}}
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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'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1XLS is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLS OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15610733 15610733]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15610733 15610733]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: xenobiotic]]
[[Category: xenobiotic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:56:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:11:30 2008''

Revision as of 13:11, 20 March 2008

Image:1xls.gif


PDB ID 1xls

Drag the structure with the mouse to rotate
, resolution 2.96Å
Ligands: and
Gene: human (Homo sapiens), mouse (Mus musculus)
Coordinates: save as pdb, mmCIF, xml



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. 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

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