6hu6: Difference between revisions

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-'''Unreleased structure'''
-The entry 6hu6 is ON HOLD  until sometime in the future
+==Structure of ARF1 RNA==
+<StructureSection load='6hu6' size='340' side='right' caption='[[6hu6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6hu6]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HU6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HU6 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</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=6hu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hu6 OCA], [http://pdbe.org/6hu6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hu6 RCSB], [http://www.ebi.ac.uk/pdbsum/6hu6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hu6 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+During mRNA localization, RNA-binding proteins interact with specific structured mRNA localization motifs. Although several such motifs have been identified, we have limited structural information on how these interact with RNA-binding proteins. Staufen proteins bind structured mRNA motifs through dsRNA-binding domains (dsRBD) and are involved in mRNA localization in Drosophila and mammals. We solved the structure of two dsRBDs of human Staufen1 in complex with a physiological dsRNA sequence. We identified interactions between the dsRBDs and the RNA sugar-phosphate backbone and direct contacts of conserved Staufen residues to RNA bases. Mutating residues mediating nonspecific backbone interactions only affected Staufen function in Drosophila when in vitro binding was severely reduced. Conversely, residues involved in base-directed interactions were required in vivo even when they minimally affected in vitro binding. Our work revealed that Staufen can read sequence features in the minor groove of dsRNA and suggests that these influence target selection in vivo.
-Authors:
+The crystal structure of Staufen1 in complex with a physiological RNA sheds light on substrate selectivity.,Lazzaretti D, Bandholz-Cajamarca L, Emmerich C, Schaaf K, Basquin C, Irion U, Bono F Life Sci Alliance. 2018 Oct 18;1(5):e201800187. doi: 10.26508/lsa.201800187., eCollection 2018 Oct. PMID:30456389<ref>PMID:30456389</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6hu6" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Bandholz-Cajamarca, L]]
+[[Category: Bono, F]]
+[[Category: Emmerich, C]]
+[[Category: Lazzaretti, D]]
+[[Category: Dsrbd]]
+[[Category: Rna]]
+[[Category: Rna localization]]
+[[Category: Smd]]
+[[Category: Staufen]]