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3x1o

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==Crystal structure of the ROQ domain of human Roquin==
==Crystal structure of the ROQ domain of human Roquin==
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<StructureSection load='3x1o' size='340' side='right' caption='[[3x1o]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='3x1o' size='340' side='right'caption='[[3x1o]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3x1o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X1O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3X1O FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3x1o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3X1O FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.201&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4txa|4txa]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RC3H1, KIAA2025, RNF198 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3x1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x1o OCA], [https://pdbe.org/3x1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3x1o RCSB], [https://www.ebi.ac.uk/pdbsum/3x1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3x1o ProSAT]</span></td></tr>
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<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=3x1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x1o OCA], [http://pdbe.org/3x1o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3x1o RCSB], [http://www.ebi.ac.uk/pdbsum/3x1o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3x1o ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/RC3H1_HUMAN RC3H1_HUMAN]] Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF and in many more mRNAs (By similarity). Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs (By similarity). In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity (By similarity). In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression (By similarity). Also recognizes CDE in its own mRNA and in that of paralogous RC3H2, possibly leading to feedback loop regulation (By similarity).
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[https://www.uniprot.org/uniprot/RC3H1_HUMAN RC3H1_HUMAN] Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF and in many more mRNAs (By similarity). Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs (By similarity). In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity (By similarity). In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression (By similarity). Also recognizes CDE in its own mRNA and in that of paralogous RC3H2, possibly leading to feedback loop regulation (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Roquin is an RNA-binding protein that prevents autoimmunity and inflammation via repression of bound target mRNAs such as inducible costimulator (Icos). When Roquin is absent or mutated (Roquin(san)), Icos is overexpressed in T cells. Here we show that Roquin enhances Dicer-mediated processing of pre-miR-146a. Roquin also directly binds Argonaute2, a central component of the RNA-induced silencing complex, and miR-146a, a microRNA that targets Icos mRNA. In the absence of functional Roquin, miR-146a accumulates in T cells. Its accumulation is not due to increased transcription or processing, rather due to enhanced stability of mature miR-146a. This is associated with decreased 3' end uridylation of the miRNA. Crystallographic studies reveal that Roquin contains a unique HEPN domain and identify the structural basis of the 'san' mutation and Roquin's ability to bind multiple RNAs. Roquin emerges as a protein that can bind Ago2, miRNAs and target mRNAs, to control homeostasis of both RNA species.
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Roquin binds microRNA-146a and Argonaute2 to regulate microRNA homeostasis.,Srivastava M, Duan G, Kershaw NJ, Athanasopoulos V, Yeo JH, Ose T, Hu D, Brown SH, Jergic S, Patel HR, Pratama A, Richards S, Verma A, Jones EY, Heissmeyer V, Preiss T, Dixon NE, Chong MM, Babon JJ, Vinuesa CG Nat Commun. 2015 Feb 20;6:6253. doi: 10.1038/ncomms7253. PMID:25697406<ref>PMID:25697406</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3x1o" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Alderton, D]]
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[[Category: Large Structures]]
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[[Category: Berrow, N S]]
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[[Category: Alderton D]]
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[[Category: Cockburn, J B]]
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[[Category: Berrow NS]]
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[[Category: Jones, E Y]]
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[[Category: Cockburn JB]]
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[[Category: Ose, T]]
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[[Category: Jones EY]]
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[[Category: Owens, R J]]
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[[Category: Ose T]]
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[[Category: Stuart, D]]
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[[Category: Owens RJ]]
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[[Category: Verma, A]]
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[[Category: Stuart D]]
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[[Category: Cytosol]]
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[[Category: Verma A]]
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[[Category: Rna]]
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[[Category: Rna binding protein]]
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[[Category: Winged-helix motif]]
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Current revision

Crystal structure of the ROQ domain of human Roquin

PDB ID 3x1o

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