{'fraction_non_alphanumeric': 0.025365853658536587, 'fraction_numerical': 0.016585365853658537, 'mean_word_length': 5.452830188679245, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
The mRNA recruiting eIF4 factors involved in protein synthesis and its regulation.

The recruitment of mRNA onto the ribosome not only affects global translation, but also the spatial and temporal fine-tuning of eukaryotic translation initiation. The eukaryotic Initiation Factor 4 (eIF4) factors, namely eIF4G, eIF4E, eIF4A and eIF4B facilitates the recruitment of mRNA onto the pre-assembled 43S Pre-Initiation complex (PIC), thus leading to formation of 48S PIC. Several biochemical and genetic studies have established the roles of eIF4 factors, however, the available structural information about it is limited. While structures of some of the individual components and sub-complexes are available, the structural details of activated mRNA bound to eIF4 factors (eIF4-mRNA) is missing. Structural characterization of the eIF4-mRNA in association with the 43S PIC in different organisms is crucial for a detailed understanding of mRNA recruitment and for exploiting the structural differences for possible drug designing.