Eukaryotic initiation factor 4F

Solution structure of yeast eIF4E bound to the m7G cap and a eIF4G fragment (PDB 1RF8).[1]

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.[2][3] 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.[3]

  1. ^ Gross, John D.; Moerke, Nathan J.; von der Haar, Tobias; Lugovskoy, Alexey A.; Sachs, Alan B.; McCarthy, John E.G.; Wagner, Gerhard (2003). "Ribosome Loading onto the mRNA Cap Is Driven by Conformational Coupling between eIF4G and eIF4E". Cell. 115 (6). Elsevier BV: 739–750. doi:10.1016/s0092-8674(03)00975-9. ISSN 0092-8674. PMID 14675538.
  2. ^ Aitken CE, Lorsch JR (June 2012). "A mechanistic overview of translation initiation in eukaryotes". Nature Structural & Molecular Biology. 19 (6): 568–76. doi:10.1038/nsmb.2303. PMID 22664984. S2CID 9201095.
  3. ^ a b Merrick WC (October 2015). "eIF4F: a retrospective". The Journal of Biological Chemistry. 290 (40): 24091–9. doi:10.1074/jbc.R115.675280. PMC 4591800. PMID 26324716.

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