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| | <StructureSection load='1r1k' size='340' side='right'caption='[[1r1k]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='1r1k' size='340' side='right'caption='[[1r1k]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1r1k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chloridea_virescens Chloridea 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 [http://proteopedia.org/fgij/fg.htm?mol=1R1K FirstGlance]. <br> | + | <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> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1r20|1r20]]</div></td></tr>
| + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECR OR NR1H1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7102 Chloridea virescens])</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=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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1r1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1k OCA], [http://pdbe.org/1r1k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r1k RCSB], [http://www.ebi.ac.uk/pdbsum/1r1k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r1k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ECR_HELVI ECR_HELVI]] Receptor for ecdysone. Binds to ecdysone response elements (ECRES) (By similarity). | + | [https://www.uniprot.org/uniprot/ECR_HELVI ECR_HELVI] Receptor for ecdysone. Binds to ecdysone response elements (ECRES) (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chloridea virescens]] | + | [[Category: Heliothis virescens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Billas, I M.L]] | + | [[Category: Billas IML]] |
| - | [[Category: Garnier, J M]] | + | [[Category: Garnier J-M]] |
| - | [[Category: Iwema, T]] | + | [[Category: Iwema T]] |
| - | [[Category: Mitschler, A]] | + | [[Category: Mitschler A]] |
| - | [[Category: Moras, D]] | + | [[Category: Moras D]] |
| - | [[Category: Rochel, N]] | + | [[Category: Rochel N]] |
| - | [[Category: SPINE, Structural Proteomics in Europe]]
| + | |
| - | [[Category: Alpha-helical sandwich]]
| + | |
| - | [[Category: Heterodimer]]
| + | |
| - | [[Category: Hormone-growth factor receptor complex]]
| + | |
| - | [[Category: Nuclear receptor]]
| + | |
| - | [[Category: Spine]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Structural proteomics in europe]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| Structural highlights
Function
ECR_HELVI Receptor for ecdysone. Binds to ecdysone response elements (ECRES) (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Billas IM, Iwema T, Garnier JM, Mitschler A, Rochel N, Moras D. Structural adaptability in the ligand-binding pocket of the ecdysone hormone receptor. Nature. 2003 Nov 6;426(6962):91-6. Epub 2003 Nov 2. PMID:14595375 doi:10.1038/nature02112
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