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PDBsum entry 1ap8
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References listed in PDB file
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Key reference
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Title
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Structure of translation factor eif4e bound to m7gdp and interaction with 4e-Binding protein.
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Authors
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H.Matsuo,
H.Li,
A.M.Mcguire,
C.M.Fletcher,
A.C.Gingras,
N.Sonenberg,
G.Wagner.
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Ref.
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Nat Struct Biol, 1997,
4,
717-724.
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PubMed id
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Abstract
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eIF4E, the mRNA cap binding protein, is a master switch that controls eukaryotic
translation. To be active, it must bind eIF4G and form the eIF4F complex, which
also contains eIF4A. Translation is downregulated by association of eIF4E with
4E-BP, which occupies the eIF4G binding site. Signalling events acting on 4E-BP
cause it to dissociate from eIF4E, and eIF4E is then free to bind eIF4G to form
the active eIF4F complex. We have solved the structure of the yeast eIF4E/m7Gpp
complex in a CHAPS micelle. We determined the position of the second nucleotide
in a complex with m7GpppA, and identified the 4E-BP binding site. eIF4E has a
curved eight-stranded antiparallel beta-sheet, decorated with three helices on
the convex face and three smaller helices inserted in connecting loops. The m7G
of the cap is intercalated into a stack of tryptophans in the concave face. The
4E-BP binding site is located in a region encompassing one edge of the
beta-sheet, the adjacent helix a2 and several regions of non-regular secondary
structure. It is adjacent to, but does not overlap the cap-binding site.
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