1ku6

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(New page: 200px<br /><applet load="1ku6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ku6, resolution 2.50&Aring;" /> '''Fasciculin 2-Mouse A...)
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Revision as of 17:45, 20 November 2007


1ku6, resolution 2.50Å

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Fasciculin 2-Mouse Acetylcholinesterase Complex

Overview

The peripheral anionic site on acetylcholinesterase (AChE), located at the, active center gorge entry, encompasses overlapping binding sites for, allosteric activators and inhibitors; yet, the molecular mechanisms, coupling this site to the active center at the gorge base to modulate, catalysis remain unclear. The peripheral site has also been proposed to be, involved in heterologous protein associations occurring during, synaptogenesis or upon neurodegeneration. A novel crystal form of mouse, AChE, combined with spectrophotometric analyses of the crystals, enabled, us to solve unique structures of AChE with a free peripheral site, and as, three complexes with peripheral site inhibitors: the, phenylphenanthridinium ligands, decidium and propidium, and the pyrogallol, ligand, gallamine, at 2.20-2.35 A resolution. Comparison with structures, of AChE complexes with the peptide fasciculin or with organic bifunctional, inhibitors unveils new structural determinants contributing to ligand, interactions at the peripheral site, and permits a detailed topographic, delineation of this site. Hence, these structures provide templates for, designing compounds directed to the enzyme surface that modulate specific, surface interactions controlling catalytic activity and non-catalytic, heterologous protein associations.

About this Structure

1KU6 is a Protein complex structure of sequences from Dendroaspis angusticeps and Mus musculus with NAG and EDO as ligands. Full crystallographic information is available from OCA.

Reference

Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site., Bourne Y, Taylor P, Radic Z, Marchot P, EMBO J. 2003 Jan 2;22(1):1-12. PMID:12505979

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