Abstract
A computational protocol that combines docking, molecular dynamics, and MM-PBSA was described to guide the design of an artificial selenoenzyme based on a Ca2+-responsive recoverin (Rn) protein. The catalytically active site of glutathione peroxidase (GPx) can be precisely incorporated into the allosteric domain of Rn, leading to a high GPx activity and tightly controlled function for the catalyzed reduction of H2O2 by glutathione (GSH). These results provide important insights into how to create an enzyme-like site in non-homologous protein scaffolds. More information can be found in the Full Paper by Q. Luo et al. on page 10350.
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