1ej4
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(New page: 200px<br /><applet load="1ej4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ej4, resolution 2.25Å" /> '''COCRYSTAL STRUCTURE ...)
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Revision as of 11:55, 20 November 2007
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COCRYSTAL STRUCTURE OF EIF4E/4E-BP1 PEPTIDE
Overview
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 Structure
1EJ4 is a Protein complex structure of sequences from Mus musculus with M7G as ligand. Full crystallographic information is available from OCA.
Reference
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
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