2l2n: Difference between revisions

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 ==Backbone 1H, 13C, and 15N Chemical Shift Assignments for the first dsRBD of protein HYL1==
-<StructureSection load='2l2n' size='340' side='right'caption='[[2l2n]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='2l2n' size='340' side='right'caption='[[2l2n]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2l2n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L2N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2l2n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L2N FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2l2m|2l2m]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At1g09700, F21M12.9 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=2l2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l2n OCA], [https://pdbe.org/2l2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l2n RCSB], [https://www.ebi.ac.uk/pdbsum/2l2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l2n ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/DRB1_ARATH DRB1_ARATH]] Double-stranded RNA-binding protein involved in RNA-mediated post-transcriptional gene silencing (PTGS). Functions in the microRNAs (miRNAs) biogenesis by assisting DICER-LIKE 1 (DCL1) in the accurate processing from primary miRNAs (pri-miRNAs) to miRNAs in the nucleus. Forms a complex with SERRATE (SE) and DCL1 to promote accurate processing of pri-miRNAs by DCL1. Binds and assist DCL1 for accurate processing of precursor miRNAs (pre-miRNA). Indirectly involved in the production of trans-acting small interfering RNAs (ta-siRNAs) derived from the TAS1, TAS2 or TAS3 endogenous transcripts by participating in the production of their initiating miRNAs. Involved with argonaute 1 (AGO1) in the guide strand selection from miRNA duplexes, presumably by directional loading of the miRNA duplex (guide stand and passenger strand) onto the RNA-induced silencing complex (RISC) for passenger strand degradation. Does not participate in sense transgene-induced post-transcriptional gene silencing (S-PTGS). Involved in several plant development aspects and response to hormones through its role in miRNAs processing.<ref>PMID:11148283</ref> <ref>PMID:14722360</ref> <ref>PMID:14972688</ref> <ref>PMID:15821876</ref> <ref>PMID:16428603</ref> <ref>PMID:16889646</ref> <ref>PMID:17337628</ref> <ref>PMID:18632569</ref> <ref>PMID:19304749</ref> <ref>PMID:19861421</ref> <ref>PMID:20462493</ref> <ref>PMID:20735118</ref>
+[https://www.uniprot.org/uniprot/DRB1_ARATH DRB1_ARATH] Double-stranded RNA-binding protein involved in RNA-mediated post-transcriptional gene silencing (PTGS). Functions in the microRNAs (miRNAs) biogenesis by assisting DICER-LIKE 1 (DCL1) in the accurate processing from primary miRNAs (pri-miRNAs) to miRNAs in the nucleus. Forms a complex with SERRATE (SE) and DCL1 to promote accurate processing of pri-miRNAs by DCL1. Binds and assist DCL1 for accurate processing of precursor miRNAs (pre-miRNA). Indirectly involved in the production of trans-acting small interfering RNAs (ta-siRNAs) derived from the TAS1, TAS2 or TAS3 endogenous transcripts by participating in the production of their initiating miRNAs. Involved with argonaute 1 (AGO1) in the guide strand selection from miRNA duplexes, presumably by directional loading of the miRNA duplex (guide stand and passenger strand) onto the RNA-induced silencing complex (RISC) for passenger strand degradation. Does not participate in sense transgene-induced post-transcriptional gene silencing (S-PTGS). Involved in several plant development aspects and response to hormones through its role in miRNAs processing.<ref>PMID:11148283</ref> <ref>PMID:14722360</ref> <ref>PMID:14972688</ref> <ref>PMID:15821876</ref> <ref>PMID:16428603</ref> <ref>PMID:16889646</ref> <ref>PMID:17337628</ref> <ref>PMID:18632569</ref> <ref>PMID:19304749</ref> <ref>PMID:19861421</ref> <ref>PMID:20462493</ref> <ref>PMID:20735118</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2l2n ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-HYL1 is a double-stranded RNA binding protein involved in microRNA processing in plants. HYL1 enhances the efficiency and precision of the RNase III protein DCL1 and participates in microRNA strand selection. In this work, we dissect the contributions of the domains of HYL1 to the binding of RNA targets. We found that the first domain is the main contributor to RNA binding. Mapping of the interaction regions by nuclear magnetic resonance on the structure of HYL1 RNA-binding domains showed that the difference in binding capabilities can be traced to sequence divergence in beta2-beta3 loop. The possible role of each domain is discussed in light of previous experimental data.
-Structure and RNA interactions of the plant MicroRNA processing-associated protein HYL1.,Rasia RM, Mateos J, Bologna NG, Burdisso P, Imbert L, Palatnik JF, Boisbouvier J Biochemistry. 2010 Sep 28;49(38):8237-9. PMID:20735118<ref>PMID:20735118</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2l2n" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
 [[Category: Large Structures]]
-[[Category: Boisbouvier, J]]
+[[Category: Boisbouvier J]]
-[[Category: Bologna, N G]]
+[[Category: Bologna NG]]
-[[Category: Burdisso, P]]
+[[Category: Burdisso P]]
-[[Category: Imbert, L]]
+[[Category: Imbert L]]
-[[Category: Mateos, J L]]
+[[Category: Mateos JL]]
-[[Category: Palatnik, J F]]
+[[Category: Palatnik JF]]
-[[Category: Rasia, R M]]
+[[Category: Rasia RM]]
-[[Category: Dsrbd]]
-[[Category: Mirna]]
-[[Category: Plant protein]]
-[[Category: Rna binding protein]]