The X-ray crystallographic structure of Torpedo californica acetylcholinesterase (TcAChE) in complex with the bifunctional inhibitor NF595, a potentially new anti-Alzheimer drug, has been solved. For the first time in TcAChE, a major conformational change in the peripheral-site tryptophan residue is observed upon complexation. The observed conformational flexibility highlights the dynamic nature of protein structures and is of importance for structure-based drug design. Copyright © 2006 American Chemical Society.
Colletier, J.P., Sanson, B., Nachon, F., Gabellieri, E., Fattorusso, C., Campiani, G., et al. (2006). Conformational Flexibility in the Peripheral Site of Torpedo californica Acetylcholinesterase Revealed by the Complex Structure with a Bifunctional Inhibitor. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 128(14), 4526-4527 [10.1021/ja058683b].
Conformational Flexibility in the Peripheral Site of Torpedo californica Acetylcholinesterase Revealed by the Complex Structure with a Bifunctional Inhibitor
Campiani, Giuseppe;
2006-01-01
Abstract
The X-ray crystallographic structure of Torpedo californica acetylcholinesterase (TcAChE) in complex with the bifunctional inhibitor NF595, a potentially new anti-Alzheimer drug, has been solved. For the first time in TcAChE, a major conformational change in the peripheral-site tryptophan residue is observed upon complexation. The observed conformational flexibility highlights the dynamic nature of protein structures and is of importance for structure-based drug design. Copyright © 2006 American Chemical Society.File | Dimensione | Formato | |
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https://hdl.handle.net/11365/8190
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