2ltr: Difference between revisions
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==Solution structure of RDE-4(32-136)== | |||
=== | <StructureSection load='2ltr' size='340' side='right' caption='[[2ltr]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ltr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LTR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LTR FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lts|2lts]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rde-4, T20G5.11 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ltr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ltr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ltr RCSB], [http://www.ebi.ac.uk/pdbsum/2ltr PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caeel]] | [[Category: Caeel]] | ||
[[Category: Chiliveri, S | [[Category: Chiliveri, S]] | ||
[[Category: Deshmukh, M | [[Category: Deshmukh, M]] | ||
[[Category: Dsrbd1]] | [[Category: Dsrbd1]] | ||
[[Category: Rde-4]] | [[Category: Rde-4]] | ||
Revision as of 06:52, 22 December 2014
Solution structure of RDE-4(32-136)
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