Evidence NMR Analysis of eIF4G1 1-249 secondary structure based on 13C chemical shifts, T1/T2 15N relaxation times and residual dipolar couplings (RDCs) revealed the presence of an alpha-helix within BOX3. eIF4G1 1-249 is predominantly disordered except for an alpha-helix in BOX3 (PMID: 36213119).Reference
Evidence NMR The amide protons of the eIF4G1 393-490 fragment exhibited few, if any, structural constraints in the absence of eIF4E. (Note: the residues 393-490 in PMID:10409688 correspond to the residues 391-488 of P39935)Reference
Component of the eIF4F complex, which interacts with the mRNA cap structure and serves as an initial point of assembly for the translation apparatus. Stimulates translation by interaction with polyadenylate-binding protein PAB1, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. TIF4631 is probably essential when TIF4632 is missing.