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
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