   2.7.7.84 | more |
inhibitor screening and identification of 12 compounds exerting competitive inhibition in the ATP binding site1 of OAS1 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors; inhibitor screening and identification of 18 compounds exerting competitive inhibition in the ATP binding site of OAS2 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors; inhibitor screening and identification of 7 compounds exerting competitive inhibition in the ATP binding site of OAS3 protein, independently of the activation state of the enzyme, docking and interaction study. Although there is little correlation between specific chemical fragments and their interactions, intermolecular contacts with OAS catalytic triad and other critical amino acids are mainly promoted by heterocycles with Pi electrons and hydrogen bond acceptors |
 |
