5t47: Difference between revisions

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==Crystal structure of the D. melanogaster eIF4E-eIF4G complex==
==Crystal structure of the D. melanogaster eIF4E-eIF4G complex==
<StructureSection load='5t47' size='340' side='right' caption='[[5t47]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='5t47' size='340' side='right'caption='[[5t47]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5t47]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T47 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T47 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5t47]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T47 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5t47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t47 OCA], [http://pdbe.org/5t47 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t47 RCSB], [http://www.ebi.ac.uk/pdbsum/5t47 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t47 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5t47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t47 OCA], [https://pdbe.org/5t47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t47 RCSB], [https://www.ebi.ac.uk/pdbsum/5t47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t47 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/IF4E_DROME IF4E_DROME]] Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures.<ref>PMID:8663200</ref>
[https://www.uniprot.org/uniprot/IF4E_DROME IF4E_DROME] Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures.<ref>PMID:8663200</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Eukaryotic initiation factor 4G (eIF4G) plays a central role in translation initiation through its interactions with the cap-binding protein eIF4E. This interaction is a major drug target for repressing translation and is naturally regulated by 4E-binding proteins (4E-BPs). 4E-BPs and eIF4G compete for binding to the eIF4E dorsal surface via a shared canonical 4E-binding motif, but also contain auxiliary eIF4E-binding sequences, which were assumed to contact non-overlapping eIF4E surfaces. However, it is unknown how metazoan eIF4G auxiliary sequences bind eIF4E. Here, we describe crystal structures of human and Drosophila melanogaster eIF4E-eIF4G complexes, which unexpectedly reveal that the eIF4G auxiliary sequences bind to the lateral surface of eIF4E, using a similar mode to that of 4E-BPs. Our studies provide a molecular model of the eIF4E-eIF4G complex, shed light on the competition mechanism of 4E-BPs, and enable the rational design of selective eIF4G inhibitors to dampen dysregulated translation in disease.


The Structures of eIF4E-eIF4G Complexes Reveal an Extended Interface to Regulate Translation Initiation.,Gruner S, Peter D, Weber R, Wohlbold L, Chung MY, Weichenrieder O, Valkov E, Igreja C, Izaurralde E Mol Cell. 2016 Oct 19. pii: S1097-2765(16)30569-X. doi:, 10.1016/j.molcel.2016.09.020. PMID:27773676<ref>PMID:27773676</ref>
==See Also==
 
*[[Eukaryotic initiation factor 3D structures|Eukaryotic initiation factor 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5t47" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chung, M Y]]
[[Category: Drosophila melanogaster]]
[[Category: Gruener, S]]
[[Category: Large Structures]]
[[Category: Igreja, C]]
[[Category: Chung M-Y]]
[[Category: Izaurralde, E]]
[[Category: Gruener S]]
[[Category: Peter, D]]
[[Category: Igreja C]]
[[Category: Valkov, E]]
[[Category: Izaurralde E]]
[[Category: Weber, R]]
[[Category: Peter D]]
[[Category: Weichenrieder, O]]
[[Category: Valkov E]]
[[Category: Wohlbold, L]]
[[Category: Weber R]]
[[Category: 4e-binding protein]]
[[Category: Weichenrieder O]]
[[Category: Cap binding protein]]
[[Category: Wohlbold L]]
[[Category: Eif4f]]
[[Category: Gene regulation]]
[[Category: Translation]]
[[Category: Translation initiation]]

Latest revision as of 18:36, 6 March 2024

Crystal structure of the D. melanogaster eIF4E-eIF4G complexCrystal structure of the D. melanogaster eIF4E-eIF4G complex

Structural highlights

5t47 is a 4 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IF4E_DROME Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures.[1]

See Also

References

  1. ↑ Lavoie CA, Lachance PE, Sonenberg N, Lasko P. Alternatively spliced transcripts from the Drosophila eIF4E gene produce two different Cap-binding proteins. J Biol Chem. 1996 Jul 5;271(27):16393-8. PMID:8663200

5t47, resolution 2.20Å

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