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[[ | ==Crystal structure of MID domain from hAGO2 in complex with ATP== | ||
<StructureSection load='3qx9' size='340' side='right' caption='[[3qx9]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3qx9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QX9 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3luc|3luc]], [[3qx8|3qx8]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EIF2C2, AGO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3qx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qx9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qx9 RCSB], [http://www.ebi.ac.uk/pdbsum/3qx9 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In RNA silencing, microRNA (miRNA)-mediated translational repression occurs through mechanisms that do not invoke messenger-RNA (mRNA) target cleavage by Argonaute proteins. The nature of these mechanisms is unclear, but several recent studies have proposed that a direct interaction between the mRNA-cap and the middle (MID) domain of Argonautes is involved. Here, we present crystallographic and NMR data demonstrating that cap analogues do not bind significantly to the isolated MID domain of human Argonaute 2 (hAGO2) and are found in the miRNA 5'-nucleotide binding site in an implausible binding mode. Additionally, in vitro pull-down experiments with full-length hAGO2 indicate that the interaction with cap analogues is nonspecific. | |||
Structural analysis of 5'-mRNA-cap interactions with the human AGO2 MID domain.,Frank F, Fabian MR, Stepinski J, Jemielity J, Darzynkiewicz E, Sonenberg N, Nagar B EMBO Rep. 2011 Apr 8. PMID:21475248<ref>PMID:21475248</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Argonaute|Argonaute]] | |||
*[[Eukaryotic initiation factor|Eukaryotic initiation factor]] | *[[Eukaryotic initiation factor|Eukaryotic initiation factor]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Darzynkiewicz, E | [[Category: Darzynkiewicz, E]] | ||
[[Category: Fabian, M R | [[Category: Fabian, M R]] | ||
[[Category: Frank, F | [[Category: Frank, F]] | ||
[[Category: Jemielity, J | [[Category: Jemielity, J]] | ||
[[Category: Nagar, B | [[Category: Nagar, B]] | ||
[[Category: Sonenberg, N | [[Category: Sonenberg, N]] | ||
[[Category: Stepinski, J | [[Category: Stepinski, J]] | ||
[[Category: Rna binding protein]] | [[Category: Rna binding protein]] | ||
[[Category: Rossmann-like fold]] | [[Category: Rossmann-like fold]] | ||
Revision as of 13:52, 9 December 2014
Crystal structure of MID domain from hAGO2 in complex with ATPCrystal structure of MID domain from hAGO2 in complex with ATP
Structural highlights
Publication Abstract from PubMedIn RNA silencing, microRNA (miRNA)-mediated translational repression occurs through mechanisms that do not invoke messenger-RNA (mRNA) target cleavage by Argonaute proteins. The nature of these mechanisms is unclear, but several recent studies have proposed that a direct interaction between the mRNA-cap and the middle (MID) domain of Argonautes is involved. Here, we present crystallographic and NMR data demonstrating that cap analogues do not bind significantly to the isolated MID domain of human Argonaute 2 (hAGO2) and are found in the miRNA 5'-nucleotide binding site in an implausible binding mode. Additionally, in vitro pull-down experiments with full-length hAGO2 indicate that the interaction with cap analogues is nonspecific. Structural analysis of 5'-mRNA-cap interactions with the human AGO2 MID domain.,Frank F, Fabian MR, Stepinski J, Jemielity J, Darzynkiewicz E, Sonenberg N, Nagar B EMBO Rep. 2011 Apr 8. PMID:21475248[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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