Coupled folding during translation initiation.
The structure of the eukaryotic initiation factor eIF4E bound to a cognate domain of eIF4G and m(7)GDP in this issue of Cell shows that these factors undergo coupled folding to form a stable complex with high cap binding activity that promotes efficient ribosomal attachment to mRNA during translation initiation.
Pestova
Tatyana V
TV
Department of Microbiology and Immunology, State University of New York Downstate Medical Center, Brooklyn, NY 11203, USA.
Hellen
Christopher U T
CU
D000818:Animals; D001665:Binding Sites / Q000235:genetics; D039561:Eukaryotic Initiation Factor-4E / Q000235:genetics / Q000378:metabolism*; D039603:Eukaryotic Initiation Factor-4G / Q000235:genetics / Q000378:metabolism*; D006153:Guanosine Diphosphate / Q000378:metabolism*; D006801:Humans; D046911:Macromolecular Substances; D014176:Protein Biosynthesis / Q000235:genetics*; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000235:genetics; D012315:RNA Caps / Q000235:genetics; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism*
D039561:Eukaryotic Initiation Factor-4E; D039603:Eukaryotic Initiation Factor-4G; D046911:Macromolecular Substances; D012315:RNA Caps; D012333:RNA, Messenger; D006153:Guanosine Diphosphate