View source for 6xww


==Constitutive decay element CDE1 from human 3'UTR==
<StructureSection load='6xww' size='340' side='right'caption='[[6xww]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xww]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XWW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XWW FirstGlance]. <br>
</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=6xww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xww OCA], [http://pdbe.org/6xww PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xww RCSB], [http://www.ebi.ac.uk/pdbsum/6xww PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xww ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Adenylate/uridylate-rich elements (AREs) are the most common cis-regulatory elements in the 3'-untranslated region (UTR) of mRNAs, where they fine-tune turnover by mediating mRNA decay. They increase plasticity and efficacy of mRNA regulation and are recognized by several ARE-specific RNA-binding proteins (RBPs). Typically, AREs are short linear motifs with a high content of complementary A and U nucleotides and often occur in multiple copies. Although thermodynamically rather unstable, the high AU-content might enable transient secondary structure formation and modify mRNA regulation by RBPs. We have recently suggested that the immunoregulatory RBP Roquin recognizes folded AREs as constitutive decay elements (CDEs), resulting in shape-specific ARE-mediated mRNA degradation. However, the structural evidence for a CDE-like recognition of AREs by Roquin is still lacking. We here present structures of CDE-like folded AREs, both in their free and protein-bound form. Moreover, the AREs in the UCP3 3'-UTR are additionally bound by the canonical ARE-binding protein AUF1 in their linear form, adopting an alternative binding-interface compared to the recognition of their CDE structure by Roquin. Strikingly, our findings thus suggest that AREs can be recognized in multiple ways, allowing control over mRNA regulation by adapting distinct conformational states, thus providing differential accessibility to regulatory RBPs.

Structural basis for the recognition of transiently structured AU-rich elements by Roquin.,Binas O, Tants JN, Peter SA, Janowski R, Davydova E, Braun J, Niessing D, Schwalbe H, Weigand JE, Schlundt A Nucleic Acids Res. 2020 Jun 3. pii: 5850806. doi: 10.1093/nar/gkaa465. PMID:32491174<ref>PMID:32491174</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Binas, O]]
[[Category: Schwalbe, H]]
[[Category: Hairpin roquin binding]]
[[Category: Rna]]