7B0V
Crystal Structure of human monoamine oxidase B in complex with (E)-3-phenyl-1-(3-(trifluoromethyl)phenyl)prop-2-en-1-one
Summary for 7B0V
| Entry DOI | 10.2210/pdb7b0v/pdb |
| Descriptor | Amine oxidase [flavin-containing] B, FLAVIN-ADENINE DINUCLEOTIDE, (E)-3-phenyl-1-(3-(trifluoromethyl)phenyl)prop-2-en-1-one, ... (6 entities in total) |
| Functional Keywords | monoamine oxidase, drug target, neurodegeneration, flavin, chalcone, mitochondrial membrane, flavoprotein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 120656.36 |
| Authors | Iacovino, L.G.,Binda, C. (deposition date: 2020-11-23, release date: 2021-11-03, Last modification date: 2024-01-31) |
| Primary citation | Iacovino, L.G.,Pinzi, L.,Facchetti, G.,Bortolini, B.,Christodoulou, M.S.,Binda, C.,Rastelli, G.,Rimoldi, I.,Passarella, D.,Di Paolo, M.L.,Dalla Via, L. Promising Non-cytotoxic Monosubstituted Chalcones to Target Monoamine Oxidase-B. Acs Med.Chem.Lett., 12:1151-1158, 2021 Cited by PubMed Abstract: A library of monosubstituted chalcones (-) bearing electron-donating and electron-withdrawing groups on both aromatic rings were selected. The cell viability on human tumor cell lines was evaluated first. The compounds unable to induce detectable cytotoxicity (, , and ) were tested using the monoamine oxidase (MAO) activity assay. Interestingly, they inhibit MAO-B, acting as competitive inhibitors, with and showing the best profiles. In particular, exhibited a potency higher than that of safinamide, taken as a reference. Docking studies and crystallographic analysis showed that in human MAO-B binds with the halogen-substituted aromatic ring in the entrance cavity, similar to safinamide, whereas is accommodated in the opposite way. The main conclusion of this cell biology, biochemistry, and structural study is to highlights as a chalcone derivative that is worth consideration for the development of novel MAO-B-selective inhibitors for the treatment of neurodegenerative diseases. PubMed: 34262643DOI: 10.1021/acsmedchemlett.1c00238 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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