4ozt: Difference between revisions
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==crystal structure of the ligand binding domains of the Bovicola ovis ecdysone receptor EcR/USP heterodimer (PonA crystal)== | ==crystal structure of the ligand binding domains of the Bovicola ovis ecdysone receptor EcR/USP heterodimer (PonA crystal)== | ||
<StructureSection load='4ozt' size='340' side='right' caption='[[4ozt]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='4ozt' size='340' side='right' caption='[[4ozt]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEQ:N-ETHYLMALEIMIDE'>NEQ</scene>, <scene name='pdbligand=P1A:2,3,14,20,22-PENTAHYDROXYCHOLEST-7-EN-6-ONE'>P1A</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEQ:N-ETHYLMALEIMIDE'>NEQ</scene>, <scene name='pdbligand=P1A:2,3,14,20,22-PENTAHYDROXYCHOLEST-7-EN-6-ONE'>P1A</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ozr|4ozr]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ozr|4ozr]]</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=4ozt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ozt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ozt RCSB], [http://www.ebi.ac.uk/pdbsum/4ozt PDBsum]</span></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=4ozt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ozt OCA], [http://pdbe.org/4ozt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ozt RCSB], [http://www.ebi.ac.uk/pdbsum/4ozt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ozt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ozt" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Retinoid X receptor|Retinoid X receptor]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 11:58, 11 August 2016
crystal structure of the ligand binding domains of the Bovicola ovis ecdysone receptor EcR/USP heterodimer (PonA crystal)crystal structure of the ligand binding domains of the Bovicola ovis ecdysone receptor EcR/USP heterodimer (PonA crystal)
Structural highlights
Publication Abstract from PubMedThe heterodimeric ligand-binding region of the Bovicola ovis ecdysone receptor has been crystallized either in the presence of an ecdysteroid or a synthetic methylene lactam insecticide. Two X-ray crystallographic structures, determined at 2.7 A resolution, show that the ligand-binding domains of both subunits of this receptor, like those of other nuclear receptors, can display significant conformational flexibility. Thermal melt experiments show that while ponasterone A stabilizes the higher order structure of the heterodimer in solution, the methylene lactam destabilizes it. The conformations of the EcR and USP subunits observed in the structure crystallized in the presence of the methylene lactam have not been seen previously in any ecdysone receptor structure and represent a new level of conformational flexibility for these important receptors. Interestingly, the new USP conformation presents an open, unoccupied ligand-binding pocket. Unprecedented conformational flexibility revealed in the ligand-binding domains of the Bovicola ovis ecdysone receptor (EcR) and ultraspiracle (USP) subunits.,Ren B, Peat TS, Streltsov VA, Pollard M, Fernley R, Grusovin J, Seabrook S, Pilling P, Phan T, Lu L, Lovrecz GO, Graham LD, Hill RJ Acta Crystallogr D Biol Crystallogr. 2014 Jul 1;70(Pt 7):1954-64. doi:, 10.1107/S1399004714009626. Epub 2014 Jun 29. PMID:25004972[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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