1rk8: Difference between revisions

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New page: left|200px<br /><applet load="1rk8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rk8, resolution 1.90Å" /> '''Structure of the cyt...
 
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[[Image:1rk8.gif|left|200px]]<br /><applet load="1rk8" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1rk8.gif|left|200px]]<br /><applet load="1rk8" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1rk8, resolution 1.90&Aring;" />
caption="1rk8, resolution 1.90&Aring;" />
'''Structure of the cytosolic protein PYM bound to the Mago-Y14 core of the exon junction complex'''<br />
'''Structure of the cytosolic protein PYM bound to the Mago-Y14 core of the exon junction complex'''<br />


==Overview==
==Overview==
The exon junction complex (EJC) is deposited on mRNAs as a consequence of, splicing and influences postsplicing mRNA metabolism. The Mago-Y14, heterodimer is a core component of the EJC. Recently, the protein PYM has, been identified as an interacting partner of Mago-Y14. Here we show that, PYM is a cytoplasmic RNA-binding protein that is excluded from the nucleus, by Crm1. PYM interacts directly with Mago-Y14 by means of its N-terminal, domain. The crystal structure of the Drosophila ternary complex at 1.9 A, resolution reveals that PYM binds Mago and Y14 simultaneously, capping, their heterodimerization interface at conserved surface residues., Formation of this ternary complex is also observed with the human, proteins. Mago residues involved in the interaction with PYM have been, implicated in nonsense-mediated mRNA decay (NMD). Consistently, human PYM, is active in NMD tethering assays. Together, these data suggest a role for, PYM in NMD.
The exon junction complex (EJC) is deposited on mRNAs as a consequence of splicing and influences postsplicing mRNA metabolism. The Mago-Y14 heterodimer is a core component of the EJC. Recently, the protein PYM has been identified as an interacting partner of Mago-Y14. Here we show that PYM is a cytoplasmic RNA-binding protein that is excluded from the nucleus by Crm1. PYM interacts directly with Mago-Y14 by means of its N-terminal domain. The crystal structure of the Drosophila ternary complex at 1.9 A resolution reveals that PYM binds Mago and Y14 simultaneously, capping their heterodimerization interface at conserved surface residues. Formation of this ternary complex is also observed with the human proteins. Mago residues involved in the interaction with PYM have been implicated in nonsense-mediated mRNA decay (NMD). Consistently, human PYM is active in NMD tethering assays. Together, these data suggest a role for PYM in NMD.


==About this Structure==
==About this Structure==
1RK8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RK8 OCA].  
1RK8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RK8 OCA].  


==Reference==
==Reference==
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[[Category: mrna processing; rrm; rbd; nmd; oskar mrna localization]]
[[Category: mrna processing; rrm; rbd; nmd; oskar mrna localization]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:39:44 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:46 2008''