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| ==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| | #REDIRECT [[6hn6]] This PDB entry is obsolete and replaced by 6hn6 |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=''>
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| == Structural highlights ==
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| <table><tr><td colspan='2'>[[1lbd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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>
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| </td></tr><tr><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://www.rcsb.org/pdb/explore.do?structureId=1lbd RCSB], [http://www.ebi.ac.uk/pdbsum/1lbd PDBsum]</span></td></tr>
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| <table>
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| == Evolutionary Conservation ==
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| [[Image:Consurf_key_small.gif|200px|right]]
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| Check<jmol>
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| <jmolCheckbox>
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| <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lb/1lbd_consurf.spt"</scriptWhenChecked>
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| <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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| <text>to colour the structure by Evolutionary Conservation</text>
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| </jmolCheckbox>
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| </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].
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| <div style="clear:both"></div>
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| ==See Also==
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| *[[Retinoid X receptor|Retinoid X receptor]]
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| == References ==
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| <references/>
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| __TOC__
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| </StructureSection>
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| [[Category: Homo sapiens]]
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| [[Category: Bourguet, W.]]
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| [[Category: Moras, D.]]
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| [[Category: SPINE, Structural Proteomics in Europe.]]
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| [[Category: Nuclear receptor]]
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| [[Category: Spine]]
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| [[Category: Structural genomic]]
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| [[Category: Structural proteomics in europe]]
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| [[Category: Transcription factor]]
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