1r1k

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[[Image:1r1k.gif|left|200px]]
 
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==Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to ponasterone A==
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The line below this paragraph, containing "STRUCTURE_1r1k", creates the "Structure Box" on the page.
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<StructureSection load='1r1k' size='340' side='right'caption='[[1r1k]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1r1k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Heliothis_virescens Heliothis virescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R1K FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPH:L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE'>EPH</scene>, <scene name='pdbligand=P1A:2,3,14,20,22-PENTAHYDROXYCHOLEST-7-EN-6-ONE'>P1A</scene></td></tr>
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{{STRUCTURE_1r1k| PDB=1r1k | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1k OCA], [https://pdbe.org/1r1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r1k RCSB], [https://www.ebi.ac.uk/pdbsum/1r1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r1k ProSAT]</span></td></tr>
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</table>
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'''Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to ponasterone A'''
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== Function ==
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[https://www.uniprot.org/uniprot/ECR_HELVI ECR_HELVI] Receptor for ecdysone. Binds to ecdysone response elements (ECRES) (By similarity).
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== Evolutionary Conservation ==
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==Overview==
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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/r1/1r1k_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/main_output.php?pdb_ID=1r1k 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 ==
The ecdysteroid hormones coordinate the major stages of insect development, notably moulting and metamorphosis, by binding to the ecdysone receptor (EcR); a ligand-inducible nuclear transcription factor. To bind either ligand or DNA, EcR must form a heterodimer with ultraspiracle (USP), the homologue of retinoid-X receptor. Here we report the crystal structures of the ligand-binding domains of the moth Heliothis virescens EcR-USP heterodimer in complex with the ecdysteroid ponasterone A and with a non-steroidal, lepidopteran-specific agonist BYI06830 used in agrochemical pest control. The two structures of EcR-USP emphasize the universality of heterodimerization as a general mechanism common to both vertebrates and invertebrates. Comparison of the EcR structures in complex with steroidal and non-steroidal ligands reveals radically different and only partially overlapping ligand-binding pockets that could not be predicted by molecular modelling and docking studies. These findings offer new perspectives for the design of insect-specific, environmentally safe insecticides. The concept of a ligand-dependent binding pocket in EcR provides an insight into the moulding of nuclear receptors to their ligand, and has potential applications for human nuclear receptors.
The ecdysteroid hormones coordinate the major stages of insect development, notably moulting and metamorphosis, by binding to the ecdysone receptor (EcR); a ligand-inducible nuclear transcription factor. To bind either ligand or DNA, EcR must form a heterodimer with ultraspiracle (USP), the homologue of retinoid-X receptor. Here we report the crystal structures of the ligand-binding domains of the moth Heliothis virescens EcR-USP heterodimer in complex with the ecdysteroid ponasterone A and with a non-steroidal, lepidopteran-specific agonist BYI06830 used in agrochemical pest control. The two structures of EcR-USP emphasize the universality of heterodimerization as a general mechanism common to both vertebrates and invertebrates. Comparison of the EcR structures in complex with steroidal and non-steroidal ligands reveals radically different and only partially overlapping ligand-binding pockets that could not be predicted by molecular modelling and docking studies. These findings offer new perspectives for the design of insect-specific, environmentally safe insecticides. The concept of a ligand-dependent binding pocket in EcR provides an insight into the moulding of nuclear receptors to their ligand, and has potential applications for human nuclear receptors.
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==About this Structure==
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Structural adaptability in the ligand-binding pocket of the ecdysone hormone receptor.,Billas IM, Iwema T, Garnier JM, Mitschler A, Rochel N, Moras D Nature. 2003 Nov 6;426(6962):91-6. Epub 2003 Nov 2. PMID:14595375<ref>PMID:14595375</ref>
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1R1K is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Heliothis_virescens Heliothis virescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1K OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural adaptability in the ligand-binding pocket of the ecdysone hormone receptor., Billas IM, Iwema T, Garnier JM, Mitschler A, Rochel N, Moras D, Nature. 2003 Nov 6;426(6962):91-6. Epub 2003 Nov 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14595375 14595375]
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</div>
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<div class="pdbe-citations 1r1k" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Heliothis virescens]]
[[Category: Heliothis virescens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Billas, I M.L.]]
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[[Category: Billas IML]]
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[[Category: Garnier, J M.]]
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[[Category: Garnier J-M]]
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[[Category: Iwema, T.]]
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[[Category: Iwema T]]
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[[Category: Mitschler, A.]]
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[[Category: Mitschler A]]
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[[Category: Moras, D.]]
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[[Category: Moras D]]
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[[Category: Rochel, N.]]
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[[Category: Rochel N]]
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[[Category: SPINE, Structural Proteomics in Europe.]]
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[[Category: Alpha-helical sandwich]]
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[[Category: Heterodimer]]
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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 regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:10:19 2008''
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Current revision

Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to ponasterone A

PDB ID 1r1k

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