Journal
MOLECULAR SIMULATION
Volume 44, Issue 2, Pages 117-127Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/08927022.2017.1346254
Keywords
Heat shock protein 16; 3 (HSP16; 3); comparative modelling; docking and molecular dynamics simulation; MMPBSA binding free energy
Funding
- Fundamental Research Grant Scheme (FRGS) [203/CIPPM/6711439]
- Higher Institution Centre of Excellence Grant (HICoE) from the Ministry of Higher Education Malaysia (MOHE) [311/CIPPM/44001005]
- MOHE
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Mycobacterium tuberculosis (Mtb) is capable of surviving in dormancy before developing to tuberculosis (TB). One of the major challenges of TB management is the identification of patients, making TB diagnosis critical for disease management. This study focuses on the 16kDa heat shock protein (HSP16.3; a potential biomarker for latent TB infection) that is expressed during the latent phase of Mtb growth. In order to explore the dynamics and interactions of HSP16.3, the 3-D structure of HSP16.3 was built via comparative modelling. The predicted structure shows a predominantly beta-sheet dodecamer with alpha-helical folds at its N-terminal. A known protein-hydrophobic probe (1,1-Bi(4-anilino)naphthalene-5,5-disulfonic acid; bisANS) was docked to the HSP16.3 model. Interacting residues predicted from docking and MD simulations are in good accordance with experimental data reported in the literature. MMPBSA calculation from MD simulation also showed favourable binding free energy of -29.90kcal/mol, driven mainly by van der waals and non-polar solvation energies. The statistical evaluation and results from the computational study on HSP16.3 indicate the reliability of the built model, which is potentially useful for further structural studies of HSP16.3 for latent TB diagnostics.
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