Altered substrate specificity of drug-resistant human immunodeficiency virus type 1 protease.

ABSTRACT: Resistance to human immunodeficiency virus type 1 protease (HIV PR) inhibitors results primarily from the selection of multiple mutations in the protease region. Because many of these mutations are selected for the ability to decrease inhibitor binding in the active site, they also affect substrate binding and potentially substrate specificity. This work investigates the substrate specificity of a panel of clinically derived protease inhibitor-resistant HIV PR variants. To compare protease specificity, we have used positional-scanning, synthetic combinatorial peptide libraries as well as a select number of individual substrates. The subsite preferences of wild-type HIV PR determined by using the substrate libraries are consistent with prior reports, validating the use of these libraries to

SUBMITTER: Dauber DS 

PROVIDER: S-EPMC135855 | biostudies-literature | 2002 Feb

REPOSITORIES: biostudies-literature