1ku6
From Proteopedia
(New page: 200px<br /><applet load="1ku6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ku6, resolution 2.50Å" /> '''Fasciculin 2-Mouse A...) |
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| - | [[Image:1ku6.gif|left|200px]]<br /><applet load="1ku6" size=" | + | [[Image:1ku6.gif|left|200px]]<br /><applet load="1ku6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ku6, resolution 2.50Å" /> | caption="1ku6, resolution 2.50Å" /> | ||
'''Fasciculin 2-Mouse Acetylcholinesterase Complex'''<br /> | '''Fasciculin 2-Mouse Acetylcholinesterase Complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The peripheral anionic site on acetylcholinesterase (AChE), located at the | + | 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== | ==About this Structure== | ||
| - | 1KU6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1KU6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KU6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: venom]] | [[Category: venom]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:58 2008'' |
Revision as of 11:37, 21 February 2008
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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 and 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
Page seeded by OCA on Thu Feb 21 13:37:58 2008
Categories: Dendroaspis angusticeps | Mus musculus | Protein complex | Bourne, Y. | Burmeister, W. | Marchot, P. | Taylor, P. | EDO | NAG | Hydrolase | Serine esterase | Synapse | Toxin | Venom
