Substrate envelope and drug resistance: crystal structure of RO1 in complex with wild-type human immunodeficiency virus type 1 protease
Authors
Prabu-Jeyabalan, MosesKing, Nancy M.
Nalivaika, Ellen A.
Heilek-Snyder, Gabrielle
Cammack, Nick
Schiffer, Celia A.
UMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyDocument Type
Journal ArticlePublication Date
2006-03-30Keywords
CrystallographyDipeptides
Drug Resistance, Viral
HIV Protease
HIV Protease Inhibitors
Hydrogen Bonding
Chemical and Pharmacologic Phenomena
Medical Molecular Biology
Medical Pharmacology
Metadata
Show full item recordAbstract
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.Source
Antimicrob Agents Chemother. 2006 Apr;50(4):1518-21. Link to article on publisher's siteDOI
10.1128/AAC.50.4.1518-1521.2006Permanent Link to this Item
http://hdl.handle.net/20.500.14038/38982PubMed ID
16569872Related Resources
Link to article in PubMedae974a485f413a2113503eed53cd6c53
10.1128/AAC.50.4.1518-1521.2006