2lts: Difference between revisions
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==Solution structure of RDE-4(150-235)== | |||
<StructureSection load='2lts' size='340' side='right'caption='[[2lts]]' scene=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/G5EBF5_CAEEL G5EBF5_CAEEL] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:24256178</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2lts" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caenorhabditis elegans]] | |||
[[Category: Large Structures]] | |||
[[Category: Chiliveri S]] | |||
[[Category: Deshmukh M]] | |||
