1lj2
From Proteopedia
(New page: 200px<br /> <applet load="1lj2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lj2, resolution 2.38Å" /> '''Recognition of eIF4...) |
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| - | [[Image:1lj2.gif|left|200px]]<br /> | + | [[Image:1lj2.gif|left|200px]]<br /><applet load="1lj2" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1lj2" size=" | + | |
caption="1lj2, resolution 2.38Å" /> | caption="1lj2, resolution 2.38Å" /> | ||
'''Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization'''<br /> | '''Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Rotaviruses, segmented double-stranded RNA viruses, co-opt the eukaryotic | + | Rotaviruses, segmented double-stranded RNA viruses, co-opt the eukaryotic translation machinery with the aid of nonstructural protein 3 (NSP3), a rotaviral functional homolog of the cellular poly(A) binding protein (PABP). NSP3 binds to viral mRNA 3' consensus sequences and circularizes mRNA via interactions with eIF4G. Here, we present the X-ray structure of the C-terminal domain of NSP3 (NSP3-C) recognizing a fragment of eIF4GI. Homodimerization of NSP3-C yields a symmetric, elongated, largely alpha-helical structure with two hydrophobic eIF4G binding pockets at the dimer interface. Site-directed mutagenesis and isothermal titration calorimetry documented that NSP3 and PABP use analogous eIF4G recognition strategies, despite marked differences in tertiary structure. |
==About this Structure== | ==About this Structure== | ||
| - | 1LJ2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Simian_rotavirus_a/sa11 Simian rotavirus a/sa11] with AU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1LJ2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Simian_rotavirus_a/sa11 Simian rotavirus a/sa11] with <scene name='pdbligand=AU:'>AU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJ2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Simian rotavirus a/sa11]] | [[Category: Simian rotavirus a/sa11]] | ||
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
| - | [[Category: Groft, C | + | [[Category: Groft, C M.]] |
[[Category: AU]] | [[Category: AU]] | ||
[[Category: nsp3; homodimer; eif4g; rotavirus; translation; mrna; closed loop; coiled coil]] | [[Category: nsp3; homodimer; eif4g; rotavirus; translation; mrna; closed loop; coiled coil]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:22 2008'' |
Revision as of 11:45, 21 February 2008
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Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization
Overview
Rotaviruses, segmented double-stranded RNA viruses, co-opt the eukaryotic translation machinery with the aid of nonstructural protein 3 (NSP3), a rotaviral functional homolog of the cellular poly(A) binding protein (PABP). NSP3 binds to viral mRNA 3' consensus sequences and circularizes mRNA via interactions with eIF4G. Here, we present the X-ray structure of the C-terminal domain of NSP3 (NSP3-C) recognizing a fragment of eIF4GI. Homodimerization of NSP3-C yields a symmetric, elongated, largely alpha-helical structure with two hydrophobic eIF4G binding pockets at the dimer interface. Site-directed mutagenesis and isothermal titration calorimetry documented that NSP3 and PABP use analogous eIF4G recognition strategies, despite marked differences in tertiary structure.
About this Structure
1LJ2 is a Protein complex structure of sequences from Simian rotavirus a/sa11 with as ligand. Full crystallographic information is available from OCA.
Reference
Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization., Groft CM, Burley SK, Mol Cell. 2002 Jun;9(6):1273-83. PMID:12086624
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