1ejh
From Proteopedia
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==Overview== | ==Overview== | ||
| - | eIF4G uses a conserved Tyr-X-X-X-X-Leu-phi segment (where X is variable | + | 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== | ==About this Structure== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
| - | [[Category: Gingras, A | + | [[Category: Gingras, A C.]] |
[[Category: Marcotrigiano, J.]] | [[Category: Marcotrigiano, J.]] | ||
[[Category: Sonenberg, N.]] | [[Category: Sonenberg, N.]] | ||
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[[Category: eif4e/eif4gii peptide/7-methyl-gdp]] | [[Category: eif4e/eif4gii peptide/7-methyl-gdp]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:23 2008'' |
Revision as of 10:28, 21 February 2008
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EIF4E/EIF4G PEPTIDE/7-METHYL-GDP
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
1EJH is a Protein complex structure of sequences from Mus musculus with 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
Page seeded by OCA on Thu Feb 21 12:28:23 2008
