1xls

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1xls" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xls, resolution 2.96&Aring;" /> '''Crystal structure o...)
Current revision (08:51, 14 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1xls.gif|left|200px]]<br />
 
-
<applet load="1xls" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1xls, resolution 2.96&Aring;" />
 
-
'''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==
+
==Crystal structure of the mouse CAR/RXR LBD heterodimer bound to TCPOBOP and 9cRA and a TIF2 peptide containg the third LXXLL motifs==
-
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.
+
<StructureSection load='1xls' size='340' side='right'caption='[[1xls]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1xls]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XLS FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.96&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9CR:(9CIS)-RETINOIC+ACID'>9CR</scene>, <scene name='pdbligand=TCD:3,5-DICHLORO-2-{4-[(3,5-DICHLOROPYRIDIN-2-YL)OXY]PHENOXY}PYRIDINE'>TCD</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xls OCA], [https://pdbe.org/1xls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xls RCSB], [https://www.ebi.ac.uk/pdbsum/1xls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xls ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/RXRA_HUMAN RXRA_HUMAN] Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes.<ref>PMID:10195690</ref> <ref>PMID:11162439</ref> <ref>PMID:11915042</ref> <ref>PMID:20215566</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xl/1xls_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xls ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XLS OCA].
+
*[[Retinoid X receptor 3D structures|Retinoid X receptor 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
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]
+
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Protein complex]]
+
[[Category: Rattus norvegicus]]
-
[[Category: Cha, J.Y.]]
+
[[Category: Cha J-Y]]
-
[[Category: Kliewer, S.A.]]
+
[[Category: Kliewer SA]]
-
[[Category: Li, Y.]]
+
[[Category: Li Y]]
-
[[Category: Repa, J.J.]]
+
[[Category: Repa JJ]]
-
[[Category: Reynolds, R.]]
+
[[Category: Reynolds R]]
-
[[Category: Suino, K.]]
+
[[Category: Suino K]]
-
[[Category: Xu, H.E.]]
+
[[Category: Xu HE]]
-
[[Category: peng, L.]]
+
[[Category: Peng L]]
-
[[Category: REA]]
+
-
[[Category: TCD]]
+
-
[[Category: car]]
+
-
[[Category: lbd]]
+
-
[[Category: nuclear receptor]]
+
-
[[Category: xenobiotic]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:07:12 2007''
+

Current revision

Crystal structure of the mouse CAR/RXR LBD heterodimer bound to TCPOBOP and 9cRA and a TIF2 peptide containg the third LXXLL motifs

PDB ID 1xls

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xls"
Personal tools