A study of an enzyme, a human cytochrome (CYP4A22), that was believed to be inactive. In the article, the authors demonstrated that the protein indeed has catalytic activity. With the use of dynamic pharmacophores, the residues important for ligand binding were discovered. Furthermore, docking was used to confirm which ligands bind to the enzyme.
Durairaj, Pradeepraj, Linbing Fan, David Machalz, Gerhard Wolber, and Matthias Bureik. “Functional Characterization and Mechanistic Modeling of the Human Cytochrome P450 Enzyme CYP4A22.” FEBS Letters 593, no. 16 (2019): 2214–25.
A study of an enzyme, a human cytochrome (CYP4A22), that was believed to be inactive. In the article, the authors demonstrated that the protein indeed has catalytic activity. With the use of dynamic pharmacophores, the residues important for ligand binding were discovered. Furthermore, docking was used to confirm which ligands bind to the enzyme.