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. 2019 May 29;12:143. doi: 10.3389/fnmol.2019.00143

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Copyright © 2019 Yeung, Georgieva, Atanasov and Tzvetkov.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Visualization of the crystal structures of hMAO-A and hMAO-B. The binding mode of irreversible and reversible MAO inhibition on the example of the most prominent MAO-A inhibitor clorgyline (irreversible) and MAO-B inhibitor safinamide (reversible) is represented. (A) Ribbon representation of the co-crystallized structure of clorgyline with the monomer hMAO-A (PDB: 2BXS, resolution: 3.15 Å). The C-terminal membrane region and the N-terminus are depicted. The surface for binding site is colored in gray transparent. (B) Representation of the covalent bonding (1.38 Å) between the irreversible MAO-A inhibitor clorgyline and the FAD co-factor. (C) Ribbon representation of the co-crystallized structure of safinamide with hMAO-B (PDB: 2V5Z, resolution: 1.6 Å). The respective chain A and B of hMAO-B dimer with FAD are depicted. (D) HYDE (HYdrogen bonding and DEsolvation) analysis of desolvation effects and interactions for safinamide (off-white). HYDE visual affinity assessment as embedded in SeeSAR: green = favorable, red = unfavorable and non-colored = no relevant for affinity. The interacting amino acid residues, important water molecules and FAD are shown. Visualization and HYDE analysis were performed using the SeeSAR tool from BioSolveIT (v.8.2, 2019).