UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Date

3-30-2006

Document Type

Article

Subjects

Crystallography; Dipeptides; Drug Resistance, Viral; HIV Protease; HIV Protease Inhibitors; Hydrogen Bonding

Disciplines

Chemical and Pharmacologic Phenomena | Medical Molecular Biology | Medical Pharmacology

Abstract

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.

Rights and Permissions

Citation: Antimicrob Agents Chemother. 2006 Apr;50(4):1518-21. Link to article on publisher's site

Related Resources

Link to article in PubMed

PubMed ID

16569872

 
 

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