==Conformational Flexibility in the Peripheral Site of Torpedo californica Acetylcholinesterase Revealed by the Complex Structure with a Bifunctional Inhibitor==

<StructureSection load='2cek' size='340' side='right'caption='[[2cek]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[2cek]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CEK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CEK FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=N8T:N-[8-(1,2,3,4-TETRAHYDROACRIDIN-9-YLTHIO)OCTYL]-1,2,3,4-TETRAHYDROACRIDIN-9-AMINE'>N8T</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cek OCA], [http://pdbe.org/2cek PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cek RCSB], [http://www.ebi.ac.uk/pdbsum/2cek PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cek ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/ACES_TORCA ACES_TORCA]] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The X-ray crystallographic structure of Torpedo californica acetylcholinesterase (TcAChE) in complex with the bifunctional inhibitor NF595, a potentially new anti-Alzheimer drug, has been solved. For the first time in TcAChE, a major conformational change in the peripheral-site tryptophan residue is observed upon complexation. The observed conformational flexibility highlights the dynamic nature of protein structures and is of importance for structure-based drug design.

Conformational flexibility in the peripheral site of Torpedo californica acetylcholinesterase revealed by the complex structure with a bifunctional inhibitor.,Colletier JP, Sanson B, Nachon F, Gabellieri E, Fattorusso C, Campiani G, Weik M J Am Chem Soc. 2006 Apr 12;128(14):4526-7. PMID:16594661<ref>PMID:16594661</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 2cek" style="background-color:#fffaf0;"></div>

==See Also==

*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]

*[[Torpedo californica acetylcholinesterase with bifunctional inhibitor|Torpedo californica acetylcholinesterase with bifunctional inhibitor]]

== References ==

<references/>

[[Category: Acetylcholinesterase]]

[[Category: Torpedo californica]]

[[Category: Gpi-anchor]]

[[Category: Synapse membrane]]