Ontology highlight
ABSTRACT:
SUBMITTER: Foulkes-Murzycki JE
PROVIDER: S-EPMC2044563 | biostudies-literature | 2007 Feb
REPOSITORIES: biostudies-literature
Foulkes-Murzycki Jennifer E JE Scott Walter Robert Peter WR Schiffer Celia A CA
Structure (London, England : 1993) 20070201 2
Hydrophobic residues outside the active site of HIV-1 protease frequently mutate in patients undergoing protease inhibitor therapy; however, the mechanism by which these mutations confer drug resistance is not understood. From analysis of molecular dynamics simulations, 19 core hydrophobic residues appear to facilitate the conformational changes that occur in HIV-1 protease. The hydrophobic core residues slide by each other, exchanging one hydrophobic van der Waal contact for another, with littl ...[more]