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| | ==Solution structure of RDE-4(150-235)== | | ==Solution structure of RDE-4(150-235)== |
| - | <StructureSection load='2lts' size='340' side='right'caption='[[2lts]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2lts' size='340' side='right'caption='[[2lts]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lts]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caeel Caeel]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LTS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lts]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LTS 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;'>[[2ltr|2ltr]]</div></td></tr> | + | </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=2lts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lts OCA], [https://pdbe.org/2lts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lts RCSB], [https://www.ebi.ac.uk/pdbsum/2lts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lts ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rde-4, T20G5.11 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=2lts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lts OCA], [https://pdbe.org/2lts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lts RCSB], [https://www.ebi.ac.uk/pdbsum/2lts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lts ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G5EBF5_CAEEL G5EBF5_CAEEL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chiliveri, S]] | + | [[Category: Chiliveri S]] |
| - | [[Category: Deshmukh, M]] | + | [[Category: Deshmukh M]] |
| - | [[Category: Dsrbd2]]
| + | |
| - | [[Category: Rde-4]]
| + | |
| - | [[Category: Rde-4dc]]
| + | |
| - | [[Category: Rna binding protein]]
| + | |
| - | [[Category: Rnai]]
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| Structural highlights
Function
G5EBF5_CAEEL
Publication Abstract from PubMed
The association of RDE-4, a protein containing two double stranded RNA binding domains (dsRBDs), with long dsRNA and Dicer (Dcr-1) initiates the siRNA pathway in C. elegans. Unlike its homologs in higher eukaryotes, RDE-4 dsRBDs possess weak (micromolar) affinity for short dsRNA. With the increasing length of dsRNA, RDE-4 exhibits enhanced affinity due to cooperativity. The linker and dsRBD2 are indispensable for RDE-4's simultaneous interaction with dsRNA and Dcr-1. Here, we present the solution structures of RDE-4 constructs that contain both dsRBDs and the linker region. In addition to the canonical dsRBD fold, both dsRBDs of RDE-4 show modified structural features such as truncation in the beta1-beta2 loop that rationalize RDE-4's relatively weak dsRNA affinity. Structure and binding studies demonstrate that dsRBD2 plays a decisive role in RDE-4:dsRNA interaction, however, contrary to previous findings, we report ephemeral interaction of RDE-4 dsRBD1 with dsRNA. More importantly, mutations in two tandem lysine residues (K217 and K218) in dsRBD2 impair RDE-4's dsRNA binding ability and could obliterate RNAi initiation in C. elegans. Additionally, our studies postulate a structural basis for the minimal requirement of linker and dsRBD2 for RDE-4's association with dsRNA and Dcr-1.
Structure of RDE-4 dsRBDs and mutational studies provide insights in the dsRNA recognition in C. elegans RNAi pathway.,Chiliveri SC, Deshmukh MV Biochem J. 2013 Nov 21. PMID:24256178[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chiliveri SC, Deshmukh MV. Structure of RDE-4 dsRBDs and mutational studies provide insights in the dsRNA recognition in C. elegans RNAi pathway. Biochem J. 2013 Nov 21. PMID:24256178 doi:http://dx.doi.org/10.1042/BJ20131347
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