2WBR

The RRM domain in GW182 proteins contributes to miRNA-mediated gene silencing


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 24 
  • Selection Criteria: LOWEST RESTRAINT VIOLATIONS 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The Rrm Domain in Gw182 Proteins Contributes to Mirna-Mediated Gene Silencing.

Eulalio, A.Tritschler, F.Buettner, R.Weichenrieder, O.Izaurralde, E.Truffault, V.

(2009) Nucleic Acids Res 37: 2974

  • DOI: https://doi.org/10.1093/nar/gkp173
  • Primary Citation of Related Structures:  
    2WBR

  • PubMed Abstract: 

    Proteins of the GW182 family interact with Argonaute proteins and are required for miRNA-mediated gene silencing. These proteins contain two structural domains, an ubiquitin-associated (UBA) domain and an RNA recognition motif (RRM), embedded in regions predicted to be unstructured. The structure of the RRM of Drosophila melanogaster GW182 reveals that this domain adopts an RRM fold, with an additional C-terminal alpha-helix. The helix lies on the beta-sheet surface, generally used by these domains to bind RNA. This, together with the absence of aromatic residues in the conserved RNP1 and RNP2 motifs, and the lack of general affinity for RNA, suggests that the GW182 RRM does not bind RNA. The domain may rather engage in protein interactions through an unusual hydrophobic cleft exposed on the opposite face of the beta-sheet. We further show that the GW182 RRM is dispensable for P-body localization and for interaction of GW182 with Argonaute-1 and miRNAs. Nevertheless, its deletion impairs the silencing activity of GW182 in a miRNA target-specific manner, indicating that this domain contributes to silencing. The conservation of structural and surface residues suggests that the RRM domain adopts a similar fold with a related function in insect and vertebrate GW182 family members.


  • Organizational Affiliation

    Max Planck Institute for Developmental Biology, Tübingen, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GW18289Drosophila melanogasterMutation(s): 0 
UniProt
Find proteins for Q8SY33 (Drosophila melanogaster)
Explore Q8SY33 
Go to UniProtKB:  Q8SY33
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UniProt GroupQ8SY33
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 24 
  • Selection Criteria: LOWEST RESTRAINT VIOLATIONS 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-03-24
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-05-15
    Changes: Data collection, Database references, Other