page_title: Eukaryotic initiation factor 4F
hierarchical_section_title: Eukaryotic initiation factor 4F
caption_attribution_description: English: NMR-based solution structure of yeast eIF4E bound to the m7G cap and a fragment of eIF4G (393-490) (PDB 1RF8). eIF4E is magenta, eIF4G is yellow, and the m7G cap is colored by element.
context_page_description: Eukaryotic initiation factor 4F is a heterotrimeric protein complex that binds the 5' cap of messenger RNAs to promote eukaryotic translation initiation. The eIF4F complex is composed of three non-identical subunits: the DEAD-box RNA helicase eIF4A, the cap-binding protein eIF4E, and the large "scaffold" protein eIF4G. The mammalian eIF4F complex was first described in 1983, and has been a major area of study into the molecular mechanisms of cap-dependent translation initiation ever since.
context_section_description: Eukaryotic initiation factor 4F (eIF4F) is a heterotrimeric protein complex that binds the 5' cap of messenger RNAs (mRNAs) to promote eukaryotic translation initiation. The eIF4F complex is composed of three non-identical subunits: the DEAD-box RNA helicase eIF4A, the cap-binding protein eIF4E, and the large "scaffold" protein eIF4G. The mammalian eIF4F complex was first described in 1983, and has been a major area of study into the molecular mechanisms of cap-dependent translation initiation ever since.
caption: Solution structure of yeast eIF4E bound to the m7G cap and a eIF4G fragment (PDB 1RF8).[1]
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