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Coupled folding during translation initiation.

Tatyana V Pestova·Christopher U T Hellen
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Abstract

The structure of the eukaryotic initiation factor eIF4E bound to a cognate domain of eIF4G and m(7)GDP in this issue of Cell shows that these factors undergo coupled folding to form a stable complex with high cap binding activity that promotes efficient ribosomal attachment to mRNA during translation initiation.

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AnimalsBinding SitesEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GGuanosine DiphosphateHumansMacromolecular SubstancesProtein BiosynthesisProtein FoldingProtein Structure, TertiaryRNA CapsRNA, MessengerCommentNews

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Tatyana V Pestova, Christopher U T Hellen. 2003-12-12. Coupled folding during translation initiation.. https://doi.org/10.1016/s0092-8674(03)00981-4

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