Can you explain Based upon the following image of imatinib bound to BCR-ABL, which of the following mutations would result in thelargest reduction in imatinib binding?Phe317☆Tyr253A. Phe317 TyrB. Tyr253 PheC. Thr315→lleD. lle313 LeuE. Phe359-TyrThr315APhe382Ile313Met290Glu286Asp381His361#Phe359

Understanding the binding interactions between imatinib and BCR-ABL is vital for anticipating the affect of changes on drug viability. The given question presents a scenario where various mutations are proposed, and the task is to determine which mutation would result in the largest reduction in imatinib binding. Analyzing the binding site interactions between imatinib and BCR-ABL is essential to make an informed decision.Answer:The correct option is C. Thr315→Ile. The Thr315 residue in the BCR-ABL kinase domain is a crucial part of the imatinib-binding pocket. A mutation from threonine (Thr) to isoleucine (Ile) is likely to disrupt the hydrogen bonding and steric interactions that contribute to the binding affinity. This substitution introduces a bulkier side chain and alters the hydrogen bonding potential, significantly impacting imatinib binding.A. Phe317 Tyr: This mutation involves a change in aromatic side chains, which may not cause a substantial reduction in imatinib binding compared to the crucial Thr315 residue.B. Tyr253 Phe: While this mutation involves an aromatic amino acid change, it is not directly in the imatinib-binding pocket and may have a lesser impact on drug binding.D. Ile313 Leu: This mutation involves a change in nonpolar side chains, which may not cause a substantial reduction in imatinib binding compared to the crucial Thr315 residue.E. Phe359-Tyr: This mutation involves a change in aromatic side chains, which may not cause a substantial reduction in imatinib binding compared to the crucial Thr315 residue.The Thr315→Ile mutation is predicted to result in the largest reduction in imatinib binding due to its location in the critical binding pocket. This analysis emphasizes the importance of specific amino acid residues in drug-protein interactions and how mutations at key sites can impact therapeutic efficacy.