3zhe
From Proteopedia
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| - | [[ | + | ==Structure of the C. elegans SMG5-SMG7 complex== |
| + | <StructureSection load='3zhe' size='340' side='right' caption='[[3zhe]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3zhe]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZHE FirstGlance]. <br> | ||
| + | </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=3zhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zhe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zhe RCSB], [http://www.ebi.ac.uk/pdbsum/3zhe PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The nonsense-mediated mRNA decay (NMD) pathway triggers the rapid degradation of aberrant mRNAs containing premature translation termination codons (PTCs). In metazoans, NMD requires three 14-3-3-like proteins: SMG5, SMG6, and SMG7. These proteins are recruited to PTC-containing mRNAs through the interaction of their 14-3-3-like domains with phosphorylated UPF1, the central NMD effector. Recruitment of SMG5, SMG6, and SMG7 causes NMD target degradation. In this study, we report the crystal structure of the Caenorhabditis elegans SMG5-SMG7 complex. The 14-3-3-like phosphopeptide recognition domains of SMG5 and SMG7 heterodimerize in an unusual perpendicular back-to-back orientation in which the peptide-binding sites face opposite directions. Structure-based mutants and functional assays indicate that the SMG5-SMG7 interaction is conserved and is crucial for efficient NMD in human cells. Notably, we demonstrate that heterodimerization increases the affinity of the SMG5-SMG7 complex for UPF1. Furthermore, we show that the degradative activity of the SMG5-SMG7 complex resides in SMG7 and that the SMG5-SMG7 complex and SMG6 play partially redundant roles in the degradation of aberrant mRNAs. We propose that the SMG5-SMG7 complex binds to phosphorylated UPF1 with high affinity and recruits decay factors to the mRNA target through SMG7, thus promoting target degradation. | ||
| - | + | An unusual arrangement of two 14-3-3-like domains in the SMG5-SMG7 heterodimer is required for efficient nonsense-mediated mRNA decay.,Jonas S, Weichenrieder O, Izaurralde E Genes Dev. 2013 Jan 15;27(2):211-25. doi: 10.1101/gad.206672.112. PMID:23348841<ref>PMID:23348841</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
| - | [[Category: Izaurralde, E | + | [[Category: Izaurralde, E]] |
| - | [[Category: Jonas, S | + | [[Category: Jonas, S]] |
| - | [[Category: Weichenrieder, O | + | [[Category: Weichenrieder, O]] |
[[Category: Mrna-binding protein]] | [[Category: Mrna-binding protein]] | ||
[[Category: Nmd]] | [[Category: Nmd]] | ||
[[Category: Phospho-peptide binding domain]] | [[Category: Phospho-peptide binding domain]] | ||
Revision as of 14:34, 5 January 2015
Structure of the C. elegans SMG5-SMG7 complex
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