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==Crystal structure of the ligand binding domains of the Bovicola ovis ecdysone receptor EcR/USP heterodimer (methylene lactam crystal)==
<StructureSection load='4ozr' size='340' side='right' caption='[[4ozr]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ozr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OZR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OZR FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ozt|4ozt]]</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=4ozr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ozr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ozr RCSB], [http://www.ebi.ac.uk/pdbsum/4ozr PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 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<ref>PMID:25004972</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fernley, R]]
[[Category: Graham, L D]]
[[Category: Grusovin, J]]
[[Category: Hill, R J]]
[[Category: Lovrecz, G O]]
[[Category: Lu, L]]
[[Category: Peat, T S]]
[[Category: Phan, T]]
[[Category: Pilling, P]]
[[Category: Pollard, M]]
[[Category: Ren, B]]
[[Category: Seabrook, S]]
[[Category: Streltsov, V A]]
[[Category: Ecdysone receptor]]
[[Category: Heterodimer]]
[[Category: Ligand binding domain]]
[[Category: Methylene lactam]]
[[Category: Transcription]]
[[Category: Usp]]