Colletier_2006_J.Am.Chem.Soc_128_4526

Reference

Title : Conformational flexibility in the peripheral site of Torpedo californica acetylcholinesterase revealed by the complex structure with a bifunctional inhibitor - Colletier_2006_J.Am.Chem.Soc_128_4526
Author(s) : Colletier JP , Sanson B , Nachon F , Gabellieri E , Fattorusso C , Campiani G , Weik M
Ref : Journal of the American Chemical Society , 128 :4526 , 2006
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.

PubMedSearch : Colletier_2006_J.Am.Chem.Soc_128_4526
PubMedID: 16594661
Gene_locus related to this paper: torca-ACHE

Related information

Inhibitor NF595
Gene_locus NF595    torca-ACHE
Structure NF595    torca-ACHE    2CEK

Citations formats

Colletier JP, Sanson B, Nachon F, Gabellieri E, Fattorusso C, Campiani G, Weik M (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 :4526

Colletier JP, Sanson B, Nachon F, Gabellieri E, Fattorusso C, Campiani G, Weik M (2006)
Journal of the American Chemical Society 128 :4526