5K5E
Discovery and Structure-Activity Relationships of a Highly Selective Butyrylcholinesterase Inhibitor by Structure-Based Virtual Screening
Summary for 5K5E
| Entry DOI | 10.2210/pdb5k5e/pdb |
| Descriptor | Cholinesterase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | high selective inhibitor, butyrylcholinesterase, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 124139.65 |
| Authors | De la Mora, E.,Dighe, S.N.,Deora, G.S.,Ross, B.P.,Nachon, F.,Brazzolotto, X. (deposition date: 2016-05-23, release date: 2016-07-27, Last modification date: 2024-11-20) |
| Primary citation | Dighe, S.N.,Deora, G.S.,De la Mora, E.,Nachon, F.,Chan, S.,Parat, M.O.,Brazzolotto, X.,Ross, B.P. Discovery and Structure-Activity Relationships of a Highly Selective Butyrylcholinesterase Inhibitor by Structure-Based Virtual Screening. J.Med.Chem., 59:7683-7689, 2016 Cited by PubMed Abstract: Structure-based virtual screening of two libraries containing 567 981 molecules was used to discover novel, selective BuChE inhibitors, which are potentially superior symptomatic treatments in late-stage Alzheimer's disease. Compound 16 was identified as a highly selective submicromolar inhibitor of BuChE (huBuChE IC50 = 0.443 μM) with high permeability in the PAMPA-BBB model. The X-ray crystal structure of huBuChE in complex with 16 revealed the atomic-level interactions and offers opportunities for further development of the series. PubMed: 27405689DOI: 10.1021/acs.jmedchem.6b00356 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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