LAUSR

The human Monoamine oxidase B (hMAO B) is an important flavoenzyme that metabolizes several biogenic amine neurotransmitters, regulates their concentration in the living cells and is involved in different neurological disorders and diseases. MD-simulation studies of dopamine (DOP) and benzylamine (BZA) complexed hMAO B structures have revealed the conformational dynamics of the gating residues Ile199 and Phe103. In the presence of large or small size substrate (DOP or BZA) molecules the inner Ile199 gate is observed to adopt an open conformation which forces the outer Phe103 gate to adopt a close conformation and it will possibly restrict the entry of any other ligand into the protein which could be the probable reason for low affinity binding of imidazole (2BFI) inhibitors in catalytically active hMAO B enzyme.