Monoamine Oxidase Inhibition In the Light of New Structural Data
2005; Bentham Science Publishers; Volume: 1; Issue: 1 Linguagem: Inglês
10.2174/1573408052952711
ISSN1875-6662
AutoresMiguel Reyes‐Parada, Angélica Fierro, Patricio Iturriaga‐Vásquez, Bruce K. Cassels,
Tópico(s)Cholinesterase and Neurodegenerative Diseases
ResumoThe 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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