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2ltr

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{{STRUCTURE_2ltr| PDB=2ltr | SCENE= }}
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==Solution structure of RDE-4(32-136)==
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===Solution structure of RDE-4(32-136)===
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<StructureSection load='2ltr' size='340' side='right' caption='[[2ltr]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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{{ABSTRACT_PUBMED_24256178}}
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== Structural highlights ==
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<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>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lts|2lts]]</td></tr>
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<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>
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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=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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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[[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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:024256178</ref><references group="xtra"/><references/>
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</div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Caeel]]
[[Category: Caeel]]
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[[Category: Chiliveri, S.]]
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[[Category: Chiliveri, S]]
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[[Category: Deshmukh, M.]]
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[[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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