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Article

Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B.

Molecular cell - 13 Mar 2009

Tritschler Felix, Braun Joerg E, Eulalio Ana, Truffault Vincent, Izaurralde Elisa, Weichenrieder Oliver

Abstract excerpt

The DEAD box helicase DDX6/Me31B functions in translational repression and mRNA decapping. How particular RNA helicases are recruited specifically to distinct functional complexes is poorly understood. We present the crystal structure of the DDX6 C-terminal RecA-like domain bound to a highly conserved FDF sequence motif in the decapping activator EDC3. The FDF peptide adopts an alpha-helical conformation upon...

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Share to Adenosine Triphosphate
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to DEAD-box RNA Helicases

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Share to Protein Multimerization

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Source

Identifiers

PMID: 19285948
DOI: 10.1016/j.molcel.2009.02.014

Genes

DDX6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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