1hl6

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(New page: 200px<br /><applet load="1hl6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hl6, resolution 2.5&Aring;" /> '''A NOVEL MODE OF RBD-P...)
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'''A NOVEL MODE OF RBD-PROTEIN RECOGNITION IN THE Y14-MAGO COMPLEX'''<br />
'''A NOVEL MODE OF RBD-PROTEIN RECOGNITION IN THE Y14-MAGO COMPLEX'''<br />
==Overview==
==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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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 Structure==
==About this Structure==
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1HL6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HL6 OCA].
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1HL6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HL6 OCA].
==Reference==
==Reference==
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[[Category: rnp]]
[[Category: rnp]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:37:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:24 2008''

Revision as of 11:02, 21 February 2008

Image:1hl6.jpg

1hl6, resolution 2.5Å

Drag the structure with the mouse to rotate

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

Overview

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 Structure

1HL6 is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

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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