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[[Image:1gqs.png|left|200px]]


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==ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH NAP==
The line below this paragraph, containing "STRUCTURE_1gqs", creates the "Structure Box" on the page.
<StructureSection load='1gqs' size='340' side='right'caption='[[1gqs]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1gqs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetronarce_californica Tetronarce californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GQS FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SAF:3-[(1S)-1-(DIMETHYLAMINO)ETHYL]PHENOL'>SAF</scene></td></tr>
{{STRUCTURE_1gqs|  PDB=1gqs  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gqs OCA], [https://pdbe.org/1gqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gqs RCSB], [https://www.ebi.ac.uk/pdbsum/1gqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gqs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACES_TETCF ACES_TETCF] 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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gq/1gqs_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gqs ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rivastigmine, a carbamate inhibitor of acetylcholinesterase, is already in use for treatment of Alzheimer's disease under the trade name of Exelon. Rivastigmine carbamylates Torpedo californica acetylcholinesterase very slowly (k(i) = 2.0 M(-1) min(-1)), whereas the bimolecular rate constant for inhibition of human acetylcholinesterase is &gt;1600-fold higher (k(i) = 3300 M(-1) min(-1)). For human butyrylcholinesterase and for Drosophila melanogaster acetylcholinesterase, carbamylation is even more rapid (k(i) = 9 x 10(4) and 5 x 10(5) M(-1) min(-1), respectively). Spontaneous reactivation of all four conjugates is very slow, with &lt;10% reactivation being observed for the Torpedo enzyme after 48 h. The crystal structure of the conjugate of rivastigmine with Torpedo acetylcholinesterase was determined to 2.2 A resolution. It revealed that the carbamyl moiety is covalently linked to the active-site serine, with the leaving group, (-)-S-3-[1-(dimethylamino)ethyl]phenol, being retained in the "anionic" site. A significant movement of the active-site histidine (H440) away from its normal hydrogen-bonded partner, E327, was observed, resulting in disruption of the catalytic triad. This movement may provide an explanation for the unusually slow kinetics of reactivation.


===ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH NAP===
Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine.,Bar-On P, Millard CB, Harel M, Dvir H, Enz A, Sussman JL, Silman I Biochemistry. 2002 Mar 19;41(11):3555-64. PMID:11888271<ref>PMID:11888271</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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{{ABSTRACT_PUBMED_11888271}}
 
==About this Structure==
[[1gqs]] is a 1 chain structure of [[Acetylcholinesterase]] 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=1GQS OCA].


==See Also==
==See Also==
*[[AChE inhibitors and substrates|AChE inhibitors and substrates]]
*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
*[[AChE inhibitors and substrates (Part III)|AChE inhibitors and substrates (Part III)]]
== References ==
*[[Acetylcholinesterase|Acetylcholinesterase]]
<references/>
*[[Alzheimer's Disease|Alzheimer's Disease]]
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
<ref group="xtra">PMID:011888271</ref><ref group="xtra">PMID:001678899</ref><references group="xtra"/>
[[Category: Tetronarce californica]]
[[Category: Acetylcholinesterase]]
[[Category: Bar-on P]]
[[Category: Torpedo californica]]
[[Category: Dvir H]]
[[Category: Bar-on, P.]]
[[Category: Enz A]]
[[Category: Dvir, H.]]
[[Category: Harel M]]
[[Category: Enz, A.]]
[[Category: Millard CB]]
[[Category: Harel, M.]]
[[Category: Silman I]]
[[Category: Millard, C B.]]
[[Category: Sussman JL]]
[[Category: Silman, I.]]
[[Category: Sussman, J L.]]
[[Category: Anti-alzheimer drug]]
[[Category: Hydrolase]]
[[Category: Neurotransmitter cleavage]]
Retrieved from "https://proteopedia.org/1gqs"