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http://purl.uniprot.org/citations/27773676http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27773676http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27773676http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2016.09.020"xsd:string
http://purl.uniprot.org/citations/27773676http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2016.09.020"xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Izaurralde E."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Izaurralde E."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Igreja C."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Igreja C."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Peter D."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Peter D."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Valkov E."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Valkov E."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Weber R."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Weber R."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Weichenrieder O."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Weichenrieder O."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Wohlbold L."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Wohlbold L."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Chung M.Y."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Chung M.Y."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Gruner S."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/author"Gruner S."xsd:string
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27773676http://purl.uniprot.org/core/date"2016"xsd:gYear