|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| - | ==LIGAND-BINDING DOMAIN OF THE HUMAN NUCLEAR RECEPTOR RXR-ALPHA==
| + | #REDIRECT [[6hn6]] This PDB entry is obsolete and replaced by 6hn6 |
| - | <StructureSection load='1lbd' size='340' side='right' caption='[[1lbd]], [[Resolution|resolution]] 2.70Å' scene=''>
| + | |
| - | == Structural highlights ==
| + | |
| - | <table><tr><td colspan='2'>[[1lbd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LBD FirstGlance]. <br>
| + | |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lbd OCA], [http://pdbe.org/1lbd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lbd RCSB], [http://www.ebi.ac.uk/pdbsum/1lbd PDBsum]</span></td></tr>
| + | |
| - | </table>
| + | |
| - | == Function ==
| + | |
| - | [[http://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/lb/1lbd_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/chain_selection.php?pdb_ID=2ata ConSurf].
| + | |
| - | <div style="clear:both"></div>
| + | |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | The crystal structure of the human retinoid-X receptor RXR-alpha ligand-binding domain reveals a previously undiscovered fold of an antiparallel alpha-helical sandwich, packed as dimeric units. Two helices and one loop form the homodimerization surface, and hydrophobic heptad repeats participate in stabilizing the fold. The existence of a ligand-binding pocket is proposed that would allow 9-cis retinoic acid to interact with different functional modules, including the AF-2 activating domain. Several lines of evidence indicate that the overall structure is a prototype fold of ligand-binding domains of nuclear receptors.
| + | |
| - | | + | |
| - | Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha.,Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D Nature. 1995 Jun 1;375(6530):377-82. PMID:7760929<ref>PMID:7760929</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 1lbd" style="background-color:#fffaf0;"></div>
| + | |
| - | | + | |
| - | ==See Also==
| + | |
| - | *[[Retinoid X receptor|Retinoid X receptor]]
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| - | __TOC__
| + | |
| - | </StructureSection>
| + | |
| - | [[Category: Human]]
| + | |
| - | [[Category: Bourguet, W]]
| + | |
| - | [[Category: Moras, D]]
| + | |
| - | [[Category: SPINE, Structural Proteomics in Europe]]
| + | |
| - | [[Category: Nuclear receptor]]
| + | |
| - | [[Category: Spine]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Structural proteomics in europe]]
| + | |
| - | [[Category: Transcription factor]]
| + | |
