Modeling of human monoamine oxidase A: from low resolution threading models to accurate comparative models based on crystal structures.
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.
Léonard
Nadia
N
Unité de Recherche en Biologie Moléculaire, Facultés Universitaires Notre-Dame de la Paix, rue de Bruxelles 61, 5000 Namur, Belgium.
Lambert
Christophe
C
Depiereux
Eric
E
Wouters
Johan
J
D000595:Amino Acid Sequence / Q000235:genetics; D000818:Animals; D003198:Computer Simulation; D003460:Crystallization; D006801:Humans; D008956:Models, Chemical; D008969:Molecular Sequence Data; D008995:Monoamine Oxidase / Q000737:chemistry* / Q000235:genetics*; D017433:Protein Structure, Secondary / Q000235:genetics; D020539:Sequence Analysis, Protein / Q000379:methods
D008995:Monoamine Oxidase