1ej4
COCRYSTAL STRUCTURE OF EIF4E/4E-BP1 PEPTIDE
OverviewOverview
eIF4G uses a conserved Tyr-X-X-X-X-Leu-phi segment (where X is variable and phi is hydrophobic) to recognize eIF4E during cap-dependent translation initiation in eukaryotes. High-resolution X-ray crystallography and complementary biophysical methods have revealed that this eIF4E recognition motif undergoes a disorder-to-order transition, adopting an L-shaped, extended chain/alpha-helical conformation when it interacts with a phylogenetically invariant portion of the convex surface of eIF4E. Inhibitors of translation initiation known as eIF4E-binding proteins (4E-BPs) contain similar eIF4E recognition motifs. These molecules are molecular mimics of eIF4G, which act by occupying the same binding site on the convex dorsum of eIF4E and blocking assembly of the translation machinery. The implications of our results for translation initiation are discussed in detail, and a molecular mechanism for relief of translation inhibition following phosphorylation of the 4E-BPs is proposed.
About this StructureAbout this Structure
1EJ4 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G., Marcotrigiano J, Gingras AC, Sonenberg N, Burley SK, Mol Cell. 1999 Jun;3(6):707-16. PMID:10394359 Page seeded by OCA on Fri May 2 15:09:50 2008