1ku6: Difference between revisions

Revision as of 11:00, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ku6.png

Template:STRUCTURE 1ku6

Fasciculin 2-Mouse Acetylcholinesterase ComplexFasciculin 2-Mouse Acetylcholinesterase Complex

Template:ABSTRACT PUBMED 12505979

About this StructureAbout this Structure

1KU6 is a Protein complex structure of sequences from Dendroaspis angusticeps and 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 Wed Jul 2 11:00:42 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Fasciculin 2-Mouse Acetylcholinesterase Complex'''
+===Fasciculin 2-Mouse Acetylcholinesterase Complex===
-==Overview==
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-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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