1EJ4

COCRYSTAL STRUCTURE OF EIF4E/4E-BP1 PEPTIDE

Summary for 1EJ4

• Entry DOI: 10.2210/pdb1ej4/pdb
• Related: 1EJ1 1EJH
• Descriptor: EUKARYOTIC INITIATION FACTOR 4E, EUKARYOTIC TRANSLATION INITIATION FACTOR 4E BINDING PROTEIN 1, 7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: eif4e/4e-bp/7-methyl-gdp, translation
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 24464.59

Authors

Marcotrigiano, J.,Gingras, A.-C.,Sonenberg, N.,Burley, S.K. (deposition date: 2000-02-28, release date: 2000-03-15, Last modification date: 2024-03-06)

Primary citation

Marcotrigiano, J.,Gingras, A.C.,Sonenberg, N.,Burley, S.K.
Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G.
Mol.Cell, 3:707-716, 1999

PubMed Abstract: 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.

PubMed: 10394359
DOI: 10.1016/S1097-2765(01)80003-4

Experimental method

X-RAY DIFFRACTION (2.25 Å)