Abstract
The recent description of the crystal structures of rat MAO-A and human MAO-B provides an unprecedented framework to elucidate the mechanisms underlying the selective interactions between these proteins and their ligands. The analysis of previous and emerging data, in the light of the structural similarities and differences between both isozymes, allows a better understanding of the requirements that determine the affinity and selectivity of substrates and inhibitors. This augurs a new impulse for the rational design of potent and selective MAO inhibitors with therapeutic potential.
Keywords: monoamine oxidase, mao inhibitors, structure-activity relationships, crystal structures
Current Enzyme Inhibition
Title: Monoamine Oxidase Inhibition In the Light of New Structural Data
Volume: 1 Issue: 1
Author(s): M. Reyes-Parada, A. Fierro, P. Iturriaga-Vasquez and B. K. Cassels
Affiliation:
Keywords: monoamine oxidase, mao inhibitors, structure-activity relationships, crystal structures
Abstract: The recent description of the crystal structures of rat MAO-A and human MAO-B provides an unprecedented framework to elucidate the mechanisms underlying the selective interactions between these proteins and their ligands. The analysis of previous and emerging data, in the light of the structural similarities and differences between both isozymes, allows a better understanding of the requirements that determine the affinity and selectivity of substrates and inhibitors. This augurs a new impulse for the rational design of potent and selective MAO inhibitors with therapeutic potential.
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Cite this article as:
Reyes-Parada M., Fierro A., Iturriaga-Vasquez P. and Cassels K. B., Monoamine Oxidase Inhibition In the Light of New Structural Data, Current Enzyme Inhibition 2005; 1 (1) . https://dx.doi.org/10.2174/1573408052952711
DOI https://dx.doi.org/10.2174/1573408052952711 |
Print ISSN 1573-4080 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-6662 |
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