1hl6: Difference between revisions

Revision as of 08:20, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1hl6.png

Template:STRUCTURE 1hl6

A NOVEL MODE OF RBD-PROTEIN RECOGNITION IN THE Y14-MAGO COMPLEXA NOVEL MODE OF RBD-PROTEIN RECOGNITION IN THE Y14-MAGO COMPLEX

Template:ABSTRACT PUBMED 12730685

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

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OCA

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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===
-==Overview==
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-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.
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 [[Category: Rdb]]
 [[Category: Rnp]]
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