Authors: D E Edmondson L DeColibus C Binda M Li A Mattevi
Publish Date: 2007/03/29
Volume: 114, Issue: 6, Pages: 703-
Abstract
Structural studies on recombinant human monoamine oxidase A hMAOA provides interesting insights on comparison with that determined for human MAOB hMAOB as well as comparison with that previously published for rat MAOA The active site cavity of hMAOA is monopartite as with rat MAOA while hMAOB is a bipartite cavity hMAOA crystallizes as a monomeric form in contrast to the dimeric forms exhibited by hMAOB and rat MAOA All of the known MAO structures show nearly identical geometries around the covalent FAD sites Differences in active site cavity structures occur away from the FAD site through conformational alterations MAOA’s and by changes in amino acid residues hMAOA and hMAOB Differences observed between human and rat MAOA’s raise questions regarding the appropriateness of the rat model in the development of MAOA specific inhibitors as drugs for eventual human use
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