Effect of sequence polymorphism and drug resistance on two HIV‐1 Gag processing sites

• Published in: European journal of biochemistry Vol. 269; no. 16; pp. 4114 - 4120
• Main Authors: Fehér, Anita, Weber, Irene T., Bagossi, Péter, Boross, Péter, Mahalingam, Bhuvaneshwari, Louis, John M., Copeland, Terry D., Torshin, Ivan Y., Harrison, Robert W., Tözsér, József
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Science Ltd 01.08.2002
• Subjects: Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Carbamates; Catalysis; Drug Resistance, Viral - genetics; Gag processing sites; Gene Products, gag - metabolism; Genes, gag; HIV Protease - chemistry; HIV Protease - genetics; HIV Protease - metabolism; HIV Protease Inhibitors - metabolism; HIV Protease Inhibitors - pharmacology; HIV-1 - drug effects; HIV-1 - genetics; HIV-1 - metabolism; HIV‐1 proteinase; Kinetics; Models, Molecular; molecular modeling; Molecular Sequence Data; oligopeptide substrates; Oligopeptides - metabolism; Polymorphism, Genetic; Protein Conformation; Substrate Specificity; Sulfonamides - pharmacology; Urea - analogs & derivatives; Urea - pharmacology

The HIV‐1 proteinase (PR) has proved to be a good target for antiretroviral therapy of AIDS, and various PR inhibitors are now in clinical use. However, there is a rapid selection of viral variants bearing mutations in the proteinase that are resistant to clinical inhibitors. Drug resistance also in...