Article
Triple Mycobacterial ATP-synthase mutations impedes Bedaquiline binding: Atomistic and structural perspectives.
Computational biology and chemistry - 1 Apr 2020
Salifu Elliasu Y, Agoni Clement, Olotu Fisayo A, Soliman Mahmoud E S
Abstract excerpt
Bedaquiline (BDQ) has demonstrated formidable bactericidal activity towards Mycobacterium tuberculosis (Mtb) in the treatment of multi-drug resistant (MDR) and extensively drug resistant (XDR) tuberculosis (TB). BDQ elicits its therapeutic function by halting the ionic shuttle of Mtb via mycobacterial F1F0 ATP-synthase blockade. However, triple mutations (L59 V, E61D and I66 M) at the ligand-binding cavity...
Topics
- Adenosine Triphosphatases
- Antitubercular Agents
- Binding Sites
- Computational Biology
- Diarylquinolines
- Enzyme Inhibitors
- Microbial Sensitivity Tests
- Models, Molecular
- Molecular Structure
- Mutation