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Structural changes in thyroid hormone receptor-beta by T3 binding and L330S mutational interactions

Central Department of Physics, Tribhuvan University, Kirtipur, Kathmandu, Nepal

Special Issues: Interdisciplinary experimental approaches for the investigation of complex systems of biophysical interest

The point mutations like L330S in the ligand binding domain (LBD) of thyroid hormone receptor-beta (THR-β) make the structural changes as reflected by Ramachandran plots, solvent accessible surface area, radial distribution functions, root mean square deviations and fluctuations, and interaction and internal energies of the LBD residues. By using nanoscale molecular dynamics (NAMD) simulations, the structural features of T3 liganded, unliganded and mutated THR-β LBD are compared to explore the molecular insights in euthyroid, hypothyroid and resistance to thyroid hormones (RTH) states, respectively. The L330S-mutant causes steric hindrance while binding T3 into THR-β LBD causing RTH in the thyroid patients.
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Keywords point mutation; thyroid hormone; thyroid hormone receptor-beta; hormone-receptor interactions; conformational changes

Citation: Tika Ram Lamichhane, Hari Prasad Lamichhane. Structural changes in thyroid hormone receptor-beta by T3 binding and L330S mutational interactions. AIMS Biophysics, 2020, 7(1): 27-40. doi: 10.3934/biophy.2020003

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