1lj2: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1lj2.gif|left|200px]] | [[Image:1lj2.gif|left|200px]] | ||
'''Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization''' | {{Structure | ||
|PDB= 1lj2 |SIZE=350|CAPTION= <scene name='initialview01'>1lj2</scene>, resolution 2.38Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=AU:GOLD ION'>AU</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1LJ2 is a [ | 1LJ2 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Simian_rotavirus_a/sa11 Simian rotavirus a/sa11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJ2 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12086624 12086624] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Simian rotavirus a/sa11]] | [[Category: Simian rotavirus a/sa11]] | ||
| Line 18: | Line 27: | ||
[[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://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:31:36 2008'' | ||
Revision as of 10:31, 20 March 2008
| |||||||||||||
| 1lj2, resolution 2.38Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | AU | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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
Page seeded by OCA on Thu Mar 20 12:31:36 2008
