3vna: Difference between revisions
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[[ | ==Structural insights into small RNA sorting and mRNA binding by Arabidopsis Ago Mid domains== | ||
<StructureSection load='3vna' size='340' side='right' caption='[[3vna]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vna]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VNA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VNA FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vnb|3vnb]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vna OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vna RCSB], [http://www.ebi.ac.uk/pdbsum/3vna PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The RISC-associated Argonaute (Ago) proteins play the catalytic role for RISC-mediated gene regulation by selecting small RNAs and subsequent targeting and cleavage of complementary mRNAs. Ago Mid domains are proposed to play essential roles in small RNA sorting. Here, we report the crystal structures of Arabidopsis Ago1 Mid domain and its chimera mutant with part of Ago1 replaced by Ago4. The structures demonstrate that a single amino insertion in the nucleotide specificity loop of AtAgo1 will change the nucleotide binding preference of AtAgo1 from "5'-U" to "5'-A". Moreover, we identify a long positively charged groove located along the "5'-end-nucleotide specificity loop" and occupied by several sulfate ions with the distance of 9-11A distance, indicating a putative mRNA target binding groove. | |||
Structural insights into small RNA sorting and mRNA target binding by Arabidopsis Argonaute Mid domains.,Zha X, Xia Q, Adam Yuan Y FEBS Lett. 2012 Sep 21;586(19):3200-7. doi: 10.1016/j.febslet.2012.06.038. Epub, 2012 Jul 3. PMID:22771475<ref>PMID:22771475</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Argonaute|Argonaute]] | |||
== | == References == | ||
[[ | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arath]] | |||
[[Category: Yuan, Y A.]] | [[Category: Yuan, Y A.]] | ||
[[Category: Zha, X.]] | [[Category: Zha, X.]] | ||
Revision as of 13:43, 16 July 2014
Structural insights into small RNA sorting and mRNA binding by Arabidopsis Ago Mid domainsStructural insights into small RNA sorting and mRNA binding by Arabidopsis Ago Mid domains
Structural highlights
Publication Abstract from PubMedThe RISC-associated Argonaute (Ago) proteins play the catalytic role for RISC-mediated gene regulation by selecting small RNAs and subsequent targeting and cleavage of complementary mRNAs. Ago Mid domains are proposed to play essential roles in small RNA sorting. Here, we report the crystal structures of Arabidopsis Ago1 Mid domain and its chimera mutant with part of Ago1 replaced by Ago4. The structures demonstrate that a single amino insertion in the nucleotide specificity loop of AtAgo1 will change the nucleotide binding preference of AtAgo1 from "5'-U" to "5'-A". Moreover, we identify a long positively charged groove located along the "5'-end-nucleotide specificity loop" and occupied by several sulfate ions with the distance of 9-11A distance, indicating a putative mRNA target binding groove. Structural insights into small RNA sorting and mRNA target binding by Arabidopsis Argonaute Mid domains.,Zha X, Xia Q, Adam Yuan Y FEBS Lett. 2012 Sep 21;586(19):3200-7. doi: 10.1016/j.febslet.2012.06.038. Epub, 2012 Jul 3. PMID:22771475[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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