Bioscience Method 2024, Vol.15, No.2, 50-57 http://bioscipublisher.com/index.php/bm 53 the drug mechanisms of protein degradation but also provide a significant basis for the design and development of drugs targeting this pathway (Kondylis et al., 2019). Figure 2 Structure of the SARS-CoV-2 N501Y mutant spike protein ectodomain bound to the ACE2 ectodomain (Adopted from Zhu et al., 2021) 2.2 Key findings and significance in the case study GPCR Drug Mechanism Elucidation: Utilizing cryo-electron microscopy, Liu et al. (2019) not only observed the precise binding sites of drug molecules to GPCRs but also captured the conformational changes following the drug-receptor interactions. These changes involve multiple structural domains and key amino acid residues of the receptor, thereby revealing the complete pathway of drug-induced activation or inhibition of GPCR signaling. These discoveries provide a novel perspective on understanding the complex physiological functions of GPCRs and bring significant value to drug development. By simulating and optimizing the binding patterns of drugs to GPCRs, drugs that are more selective and have fewer side effects can be designed, thus more effectively treating various diseases related to GPCRs, such as heart disease, neurological disorders, and cancer. Antiviral Drug Mechanism Elucidation: Cryo-electron microscopy has revealed the precise binding modes of antiviral drugs to viral proteins and deeply explored how drugs interfere with the viral life cycle. These findings include the binding kinetics of drugs to viral proteins, drug-induced conformational changes in viral proteins, and
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