Modeling of Human Monoamine Oxidase A: From Low Resolution Threading Models to Accurate Comparative Models Based on Crystal Structures

Nadia Léonard, Christophe Lambert, Eric Depiereux, Johan Wouters

Research output: Contribution to journalArticle


The recently published crystal structure of monoamine oxidase (MAO) B was a major breakthrough for structural and functional understanding of flavin containing amine oxidases: it opens a new era of research and provides new opportunities to those interested in the biochemistry and pharmacology of those important drug targets. In particular, it allowed accurate modeling of human MAO A, both proteins sharing over 70% sequence identity. In the present contribution, we summarize the efforts made in order to obtain structural information on the human MAO A, including sequence analysis, secondary structure predictions, and preliminary models obtained by fold recognition and comparative modeling based on proteins sharing low sequence identity.

Original languageEnglish
Pages (from-to)47-61
Number of pages15
Issue number1-2
Publication statusPublished - 1 Jan 2004



  • Low resolution
  • Modeling
  • Monoamine oxidase A

Cite this