1ej4: Difference between revisions

New page: left|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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[[Image:1ej4.jpg|left|200px]]<br /><applet load="1ej4" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ej4.jpg|left|200px]]<br /><applet load="1ej4" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ej4, resolution 2.25&Aring;" />
caption="1ej4, resolution 2.25&Aring;" />
'''COCRYSTAL STRUCTURE OF EIF4E/4E-BP1 PEPTIDE'''<br />
'''COCRYSTAL STRUCTURE OF EIF4E/4E-BP1 PEPTIDE'''<br />


==Overview==
==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.
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==
1EJ4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with M7G as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EJ4 OCA].  
1EJ4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=M7G:'>M7G</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EJ4 OCA].  


==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Burley, S.K.]]
[[Category: Burley, S K.]]
[[Category: Gingras, A.C.]]
[[Category: Gingras, A C.]]
[[Category: Marcotrigiano, J.]]
[[Category: Marcotrigiano, J.]]
[[Category: Sonenberg, N.]]
[[Category: Sonenberg, N.]]
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[[Category: eif4e/4e-bp/7-methyl-gdp]]
[[Category: eif4e/4e-bp/7-methyl-gdp]]


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