Article
Electrostatics Plays a Crucial Role in HIV-1 Protease Substrate Binding, Drugs Fail to Take Advantage.
Biochemistry - 15 Sept 2020
Ahsan Mohd, Pindi Chinmai, Senapati Sanjib
Abstract excerpt
HIV-1 protease (HIVPR) is an important drug target for combating AIDS. This enzyme is an aspartyl protease that is functionally active in its dimeric form. Nuclear magnetic resonance reports have convincingly shown that a pseudosymmetry exists at the HIVPR active site, where only one of the two aspartates remains protonated over the pH range of 2.5-7.0. To date, all HIVPR-targeted drug design strategies focused...
Topics
- Amino Acid Sequence
- Apoptosis
- Binding Sites
- Catalytic Domain
- Cytochromes c
- Drug Design
- HIV Protease
- Humans
- Mitochondria
- Molecular Dynamics Simulation
- Mutation
- Oligopeptides