Libro

Descripción

Human Guanine Monophosphate Synthetase (hGMPS) is identified as a potential target for anti-cancer and immunosuppressive therapies. The comparative structural bioinformatics investigations on the different crystal structures of human and non-human GMPS enzymes may provide important information about the structural properties of the enzyme. Six conserved water molecules are identified in the synthetase and eleven in the GATase domain of human and non-human GMPS. This structural information reveals the hydrophilic positions are invariant in their respective domains of the GMPS enzyme and will also help the protein crystallographer to predict the water molecules during solving the crystal structures of this protein.