First partial three-dimensional model of human monoamine oxidase A

Johan Wouters, Guy Baudoux

Résultats de recherche: Contribution à un journal/une revueArticleRevue par des pairs

Résumé

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.

langue originaleAnglais
Pages (de - à)97-110
Nombre de pages14
journalProteins: Structure, Function and Genetics
Volume32
Numéro de publication1
Les DOIs
Etat de la publicationPublié - 1 juil. 1998

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