Ontology highlight
ABSTRACT:
SUBMITTER: Yedidi RS
PROVIDER: S-EPMC4288442 | biostudies-literature | 2013 Sep
REPOSITORIES: biostudies-literature
Yedidi Ravikiran S RS Muhuhi Joseck M JM Liu Zhigang Z Bencze Krisztina Z KZ Koupparis Kyriacos K O'Connor Carrie E CE Kovari Iulia A IA Spaller Mark R MR Kovari Ladislau C LC
Biochemical and biophysical research communications 20130803 4
Multidrug-resistant (MDR) clinical isolate-769, human immunodeficiency virus type-1 (HIV-1) protease (PDB ID: 1TW7), was shown to exhibit wide-open flaps and an expanded active site cavity, causing loss of contacts with protease inhibitors. In the current study, the expanded active site cavity of MDR769 HIV-1 protease was screened with a series of peptide-inhibitors that were designed to mimic the natural substrate cleavage site, capsid/p2. Scanning Ala/Phe chemical mutagenesis approach was inco ...[more]