5DTJ
Crystal Structure of dfp-inhibited mouse acetylcholinesterase in complex with the reactivator SP-134
Summary for 5DTJ
| Entry DOI | 10.2210/pdb5dtj/pdb |
| Related | 5DTG 5DTI |
| Descriptor | Acetylcholinesterase, 1-[5-(2,4-dichlorophenoxy)pentyl]-1H-imidazole (2 entities in total) |
| Functional Keywords | hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 2 |
| Total formula weight | 121454.46 |
| Authors | Tran, T.H.,Tong, L. (deposition date: 2015-09-18, release date: 2015-10-21, Last modification date: 2023-09-27) |
| Primary citation | Katz, F.S.,Pecic, S.,Tran, T.H.,Trakht, I.,Schneider, L.,Zhu, Z.,Ton-That, L.,Luzac, M.,Zlatanic, V.,Damera, S.,Macdonald, J.,Landry, D.W.,Tong, L.,Stojanovic, M.N. Discovery of New Classes of Compounds that Reactivate Acetylcholinesterase Inhibited by Organophosphates. Chembiochem, 16:2205-2215, 2015 Cited by PubMed Abstract: Acetylcholinesterase (AChE) that has been covalently inhibited by organophosphate compounds (OPCs), such as nerve agents and pesticides, has traditionally been reactivated by using nucleophilic oximes. There is, however, a clearly recognized need for new classes of compounds with the ability to reactivate inhibited AChE with improved in vivo efficacy. Here we describe our discovery of new functional groups--Mannich phenols and general bases--that are capable of reactivating OPC--inhibited AChE more efficiently than standard oximes and we describe the cooperative mechanism by which these functionalities are delivered to the active site. These discoveries, supported by preliminary in vivo results and crystallographic data, significantly broaden the available approaches for reactivation of AChE. PubMed: 26350723DOI: 10.1002/cbic.201500348 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.71 Å) |
Structure validation
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