Torpedo californica acetylcholinesterase with bifunctional inhibitor

Conformational flexibility in the peripheral site of Torpedo californica acetylecholinesterase revealed by the complex structure with a bifunctional inhibitor (2cek)

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.