1n5r

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[[Image:1n5r.gif|left|200px]]<br /><applet load="1n5r" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1n5r.gif|left|200px]]
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caption="1n5r, resolution 2.25&Aring;" />
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'''Crystal structure of the mouse acetylcholinesterase-propidium complex'''<br />
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{{Structure
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|PDB= 1n5r |SIZE=350|CAPTION= <scene name='initialview01'>1n5r</scene>, resolution 2.25&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PRM:3,8-DIAMINO-5[3-(DIETHYLMETHYLAMMONIO)PROPYL]-6-PHENYLPHENANTHRIDINIUM'>PRM</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7]
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|GENE=
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}}
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'''Crystal structure of the mouse acetylcholinesterase-propidium complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1N5R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=P6G:'>P6G</scene>, <scene name='pdbligand=PG4:'>PG4</scene>, <scene name='pdbligand=PRM:'>PRM</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N5R OCA].
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1N5R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N5R OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12505979 12505979]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12505979 12505979]
[[Category: Acetylcholinesterase]]
[[Category: Acetylcholinesterase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: serine esterase]]
[[Category: serine esterase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:52:32 2008''

Revision as of 10:52, 20 March 2008

Image:1n5r.gif


PDB ID 1n5r

Drag the structure with the mouse to rotate
, resolution 2.25Å
Ligands: , , , and
Activity: Acetylcholinesterase, with EC number 3.1.1.7
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the mouse acetylcholinesterase-propidium 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

1N5R is a Single protein structure of sequence from Mus musculus. 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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