First partial three-dimensional model of human monoamine oxidase A

Johan Wouters, Guy Baudoux

Research output: Contribution to journalArticlepeer-review


A survey of the major known structural aspects of monoamine oxidase (MAO) is given and a first partial model of human MAO A is presented. This 3D model has been established using secondary structure predictions and fold recognition methods. It shows two α/β domains (the FAD-binding N-terminal and central domains) and an α+β domain. The C-terminal region is predicted to be responsible for anchoring the protein into the mitochondrial membrane and was not modeled. The covalent binding of the flavin cofactor to a cysteine residue is well predicted. The model is validated with experimental data from the literature and should be useful in designing new experimental studies (site-directed mutagenesis, chemical modification, specific antibodies). This first step towards the 3D structure of monoamine oxidase should contribute to a better understanding of the mechanisms of action and inhibition of this drug target in the treatment of clinical depression.

Original languageEnglish
Pages (from-to)97-110
Number of pages14
JournalProteins: Structure, Function and Genetics
Issue number1
Publication statusPublished - 1 Jul 1998


  • Flavoproteins
  • Fold prediction
  • Knowledge-based modeling
  • MAO A
  • Membrane protein
  • Secondary structure
  • Threading
  • Type A monoamine oxidase


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