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First partial three-dimensional model of human monoamine oxidase A.

Authors
  • Wouters, J
  • Baudoux, G
Type
Published Article
Journal
Proteins: Structure, Function, and Bioinformatics
Publisher
Wiley
Publication Date
Jul 01, 1998
Volume
32
Issue
1
Pages
97–110
Identifiers
PMID: 9672046
Source
Medline
License
Unknown

Abstract

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 alpha/beta domains (the FAD-binding N-terminal and central domains) and an alpha+beta 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.

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