Structure of translation factor elF4E bound to m7GDP and interaction with 4E-binding protein

@article{Matsuo1997StructureOT,
  title={Structure of translation factor elF4E bound to m7GDP and interaction with 4E-binding protein},
  author={Hiroshi Matsuo and Hanjun Li and Abigail Manson McGuire and C. Mark Fletcher and Anne-Claude Gingras and Nahum Sonenberg and Gerhard Wagner},
  journal={Nature Structural Biology},
  year={1997},
  volume={4},
  pages={717-724}
}
elF4E, the mRNA cap binding protein, is a master switch that controls eukaryotic translation. To be active, it must bind elF4G and form the elF4F complex, which also contains elF4A. Translation is downregulated by association of elF4E with 4E-BP, which occupies the elF4G binding site. Signalling events acting on 4E-BP cause it to dissociate from elF4E, and elF4E is then free to bind elF4G to form the active elF4F complex. We have solved the structure of the yeast elF4E/m7Gpp complex in a CHAPS… CONTINUE READING

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