1hl6: Difference between revisions
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{{STRUCTURE_1hl6| PDB=1hl6 | SCENE= }} | |||
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'''A NOVEL MODE OF RBD-PROTEIN RECOGNITION IN THE Y14-MAGO COMPLEX''' | '''A NOVEL MODE OF RBD-PROTEIN RECOGNITION IN THE Y14-MAGO COMPLEX''' | ||
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[[Category: Izaurralde, E.]] | [[Category: Izaurralde, E.]] | ||
[[Category: Yao, W.]] | [[Category: Yao, W.]] | ||
[[Category: | [[Category: Exon-exon junction]] | ||
[[Category: | [[Category: Nmd]] | ||
[[Category: | [[Category: Oskar]] | ||
[[Category: | [[Category: Rdb]] | ||
[[Category: | [[Category: Rnp]] | ||
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Revision as of 18:58, 2 May 2008
A NOVEL MODE OF RBD-PROTEIN RECOGNITION IN THE Y14-MAGO COMPLEX
OverviewOverview
Y14 and Mago are conserved eukaryotic proteins that associate with spliced mRNAs in the nucleus and remain associated at exon junctions during and after nuclear export. In the cytoplasm, Y14 is involved in mRNA quality control via the nonsense-mediated mRNA decay (NMD) pathway and, together with Mago, is involved in localization of osk (oskar) mRNA. We have determined the crystal structure of the complex between Drosophila melanogaster Y14 and Mago at a resolution of 2.5 A. The structure reveals an atypical mode of protein-protein recognition mediated by an RNA-binding domain (RBD). Instead of binding RNA, the RBD of Y14 engages its RNP1 and RNP2 motifs to bind Mago. Using structure-guided mutagenesis, we show that Mago is also a component of the NMD pathway, and that its association with Y14 is essential for function. Heterodimerization creates a single structural platform that interacts with the NMD machinery via phylogenetically conserved residues.
About this StructureAbout this Structure
1HL6 is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.
ReferenceReference
A novel mode of RBD-protein recognition in the Y14-Mago complex., Fribourg S, Gatfield D, Izaurralde E, Conti E, Nat Struct Biol. 2003 Jun;10(6):433-9. PMID:12730685 Page seeded by OCA on Fri May 2 18:58:19 2008