The IF2 initiation factor is a crucial component in the process of protein synthesis. The largest among the three indispensable translation initiation factors is IF-2, which possesses a molecular mass of 97 kDa. The protein has many domains, including an N-terminal domain, a GTPase domain, a linker region, C1, C2, and C-terminal domains. The GTPase domain encompasses the G1-G5 motif, which is responsible for the binding and hydrolysis of GTP. The activity of IF2 is regulated by conformational changes induced by the binding and hydrolysis of GTP. The primary function of IF-2 is to transport the initiator fMet-tRNA to the P-site of the 30S ribosomal subunit. The C2 domain of IF2 has a unique recognition and binding affinity towards the initiator tRNA. The IF-2 protein has been observed to form a ternary complex when interacting with GTP and fMet-tRNA. This complex has been found to interact with the 30S subunit. The initiation of mRNA translation involves the placement of the start codon in the P-site through the codon-anticodon base matching with the tRNA anti-codon. IF2 regulates start codon selection accuracy and inhibits elongator tRNAs' binding by selectively binding to fMet-tRNA. Additionally, it relocates the initiator tRNA on the 30S subunit to enhance the optimum contact with the P-site. Furthermore, IF2 exhibits RNA chaperone activity, which enables it to rectify misfolded RNA structures. In general, the IF2 protein plays a crucial role in coordinating many steps of translation initiation, including the binding of mRNA and fMet-tRNA to the start codon, the joining of sub-units, and the activation of GTPase.