Article
Hydrophobic sliding: a possible mechanism for drug resistance in human immunodeficiency virus type 1 protease.
Structure (London, England : 1993) - 1 Feb 2007
Foulkes-Murzycki Jennifer E, Scott Walter Robert Peter, Schiffer Celia A
Abstract excerpt
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...
Topics
- Amino Acids
- Drug Resistance, Viral
- HIV Protease
- HIV Protease Inhibitors
- Hydrogen Bonding
- Hydrophobic and Hydrophilic Interactions
- Mutation
- Protein Conformation