Department of Biochemistry and Molecular Pharmacology
Crystallography; Dipeptides; Drug Resistance, Viral; HIV Protease; HIV Protease Inhibitors; Hydrogen Bonding
Chemical and Pharmacologic Phenomena | Medical Molecular Biology | Medical Pharmacology
In our previous crystallographic studies of human immunodeficiency virus type 1 (HIV-1) protease-substrate complexes, we described a conserved "envelope" that appears to be important for substrate recognition and the selection of drug-resistant mutations. In this study, the complex of HIV-1 protease with the inhibitor RO1 was determined and comparison with the substrate envelope provides a rationale for mutational patterns.
DOI of Published Version
Antimicrob Agents Chemother. 2006 Apr;50(4):1518-21. Link to article on publisher's site
Antimicrobial agents and chemotherapy
Prabu-Jeyabalan M, King NM, Nalivaika EA, Heilek-Snyder G, Cammack N, Schiffer CA. (2006). Substrate envelope and drug resistance: crystal structure of RO1 in complex with wild-type human immunodeficiency virus type 1 protease. Open Access Publications by UMMS Authors. https://doi.org/10.1128/AAC.50.4.1518-1521.2006. Retrieved from https://escholarship.umassmed.edu/oapubs/181