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Conformational flexibility in the peripheral site of Torpedo californica acetylecholinesterase revealed by the complex structure with a bifunctional inhibitor

Overview

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.

About this Structure

2CEK is a Single protein structure of sequence from Torpedo californica with , , , and as ligands. Active as acetylcholinesterase, with EC number 3.1.1.7 Known structural/functional Site: . Full crystallographic information is available from OCA.

Down the gorge

binds both the active and peripheral sites. It is mainly bound to through pi-pi interactions. The n-carbon long linker spans the gorge.

Reference

Conformational flexibility in the peripheral site of Torpedo californica acetylcholinesterase revealed by the complex structure with a bifunctional inhibitor., Colletier JP, Sanson B, Nachon F, Gabellieri E, Fattorusso C, Campiani G, Weik M, J Am Chem Soc. 2006 Apr 12;128(14):4526-7. PMID:16594661

Page seeded by OCA on Thu Feb 21 16:47:47 2008