View source for 5fum


==Mus musculus acetylcholinesterase in complex with AL200==
<StructureSection load='5fum' size='340' side='right'caption='[[5fum]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fum]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FUM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene>, <scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene>, <scene name='pdbligand=SOF:2-(BIPHENYL-4-YLOXY)-1-[4-(4-ETHYLPIPERAZIN-1-YL)PIPERIDIN-1-YL]ETHANONE'>SOF</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fum OCA], [https://pdbe.org/5fum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fum RCSB], [https://www.ebi.ac.uk/pdbsum/5fum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fum ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACES_MOUSE ACES_MOUSE] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Vector control of disease-transmitting mosquitoes is increasingly important due to the re-emergence and spread of infections such as malaria and dengue. We have conducted a high throughput screen (HTS) of 17,500 compounds for inhibition of the essential AChE1 enzymes from the mosquitoes Anopheles gambiae and Aedes aegypti. In a differential HTS analysis including the human AChE, several structurally diverse, potent, and selective non-covalent AChE1 inhibitors were discovered. For example, a phenoxyacetamide-based inhibitor was identified with a 100-fold selectivity for the mosquito- over the human enzyme. The compound also inhibited a resistance conferring mutant of AChE1. Structure-selectivity relationships could be proposed based on the enzymes' 3D structures; the hits' selectivity profiles appear to be linked to differences in two loops that affect the structure of the entire active site. Non-covalent inhibitors of AChE1, such as the ones presented here, provide valuable starting points towards insecticides and are complementarity to existing and new covalent inhibitors.

Discovery of selective inhibitors targeting acetylcholinesterase 1 from disease-transmitting mosquitoes.,Engdahl C, Knutsson S, Ekstrom FJ, Linusson A J Med Chem. 2016 Sep 6. PMID:27598521<ref>PMID:27598521</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5fum" style="background-color:#fffaf0;"></div>

==See Also==
*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Ekstrom F]]
[[Category: Engdahl C]]
[[Category: Knutsson S]]
[[Category: Linusson A]]