View source for 4umm

==The Cryo-EM structure of the palindromic DNA-bound USP-EcR nuclear receptor reveals an asymmetric organization with allosteric domain positioning==
<StructureSection load='4umm' size='340' side='right' caption='[[4umm]], [[Resolution|resolution]] 11.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4umm]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UMM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UMM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='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=4umm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4umm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4umm RCSB], [http://www.ebi.ac.uk/pdbsum/4umm PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/ECR_HELVI ECR_HELVI]] Receptor for ecdysone. Binds to ecdysone response elements (ECRES) (By similarity). 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nuclear receptors (NRs) regulate gene expression through DNA- and ligand-binding and thus represent crucial therapeutic targets. The ultraspiracle protein/ecdysone receptor (USP/EcR) complex binds to half-sites with a one base pair spaced inverted repeat (IR1), a palindromic DNA response element (RE) reminiscent of IRs observed for vertebrate steroid hormone receptors. Here we present the cryo electron microscopy structure of the USP/EcR complex bound to an IR1 RE which provides the first description of a full IR-bound NR complex. The structure reveals that even though the DNA is almost symmetric, the complex adopts a highly asymmetric architecture in which the ligand-binding domains (LBDs) are positioned 5' off-centred. Additional interactions of the USP LBD with the 5'-flanking sequence trigger transcription activity as monitored by transfection assays. The comparison with DR-bound NR complexes suggests that DNA is the major allosteric driver in inversely positioning the LBDs, which serve as the main binding-site for transcriptional regulators.

The palindromic DNA-bound USP/EcR nuclear receptor adopts an asymmetric organization with allosteric domain positioning.,Maletta M, Orlov I, Roblin P, Beck Y, Moras D, Billas IM, Klaholz BP Nat Commun. 2014 Jun 19;5:4139. doi: 10.1038/ncomms5139. PMID:24942373<ref>PMID:24942373</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Billas, I M.L]]
[[Category: Klaholz, B P]]
[[Category: Maletta, M]]
[[Category: Moras, D]]
[[Category: Orlov, I]]
[[Category: Allostery]]
[[Category: Cryo electron microscopy]]
[[Category: Dna response element]]
[[Category: Ecdysone]]
[[Category: Nuclear receptor]]
[[Category: Transcription]]
[[Category: Usp-ecr]]