2i91: Difference between revisions
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<StructureSection load='2i91' size='340' side='right'caption='[[2i91]], [[Resolution|resolution]] 2.65Å' scene=''> | <StructureSection load='2i91' size='340' side='right'caption='[[2i91]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2i91]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2i91]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I91 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2i91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i91 OCA], [https://pdbe.org/2i91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i91 RCSB], [https://www.ebi.ac.uk/pdbsum/2i91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i91 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2i91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i91 OCA], [https://pdbe.org/2i91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i91 RCSB], [https://www.ebi.ac.uk/pdbsum/2i91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i91 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/RO60_XENLA RO60_XENLA] RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. May stabilize these RNAs from degradation. May play roles in cilia formation and/or maintenance (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Xenopus laevis]] | ||
[[Category: | [[Category: Reinisch KM]] | ||
[[Category: | [[Category: Stein AJ]] | ||
Latest revision as of 13:07, 30 August 2023
60kDa Ro autoantigen in complex with a fragment of misfolded RNA60kDa Ro autoantigen in complex with a fragment of misfolded RNA
Structural highlights
FunctionRO60_XENLA RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. May stabilize these RNAs from degradation. May play roles in cilia formation and/or maintenance (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe Ro autoantigen is ring-shaped, binds misfolded noncoding RNAs and is proposed to function in quality control. Here we determine how Ro interacts with misfolded RNAs. Binding of Ro to misfolded precursor (pre)-5S ribosomal RNA requires a single-stranded 3' end and helical elements. As mutating most sequences of the helices and tail results in modest decreases in binding, Ro may be able to associate with a range of RNAs. Ro binds several other RNAs that contain single-stranded tails. A crystal structure of Ro bound to a misfolded pre-5S rRNA fragment reveals that the tail inserts into the cavity, while a helix binds on the surface. Most contacts of Ro with the helix are to the backbone. Mutagenesis reveals that Ro has an extensive RNA-binding surface. We propose that Ro uses this surface to scavenge RNAs that fail to bind their specific RNA-binding proteins. Structural and biochemical basis for misfolded RNA recognition by the Ro autoantigen.,Fuchs G, Stein AJ, Fu C, Reinisch KM, Wolin SL Nat Struct Mol Biol. 2006 Nov;13(11):1002-9. Epub 2006 Oct 15. PMID:17041599[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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