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.
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Citation: Antimicrob Agents Chemother. 2006 Apr;50(4):1518-21. Link to article on publisher's site
Prabu-Jeyabalan, Moses; King, Nancy M.; Nalivaika, Ellen A.; Heilek-Snyder, Gabrielle; Cammack, Nick; and Schiffer, Celia A., "Substrate envelope and drug resistance: crystal structure of RO1 in complex with wild-type human immunodeficiency virus type 1 protease" (2006). Open Access Articles. Paper 181.