1lj2
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(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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Revision as of 15:55, 12 November 2007
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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 AU 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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