1j06: Difference between revisions

Revision as of 14:17, 1 July 2008

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File:1j06.png

Template:STRUCTURE 1j06

Crystal structure of mouse acetylcholinesterase in the apo formCrystal structure of mouse acetylcholinesterase in the apo form

Template:ABSTRACT PUBMED 12505979

About this StructureAbout this Structure

1J06 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 1 14:17:44 2008

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OCA

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-'''Crystal structure of mouse acetylcholinesterase in the apo form'''
+===Crystal structure of mouse acetylcholinesterase in the apo form===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12505979}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12505979}}
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 [[Category: Hydrolase fold]]
 [[Category: Serine esterase]]
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