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4ey8

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==Crystal structure of recombinant human acetylcholinesterase in complex with fasciculin-2==
==Crystal structure of recombinant human acetylcholinesterase in complex with fasciculin-2==
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<StructureSection load='4ey8' size='340' side='right' caption='[[4ey8]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<StructureSection load='4ey8' size='340' side='right'caption='[[4ey8]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ey8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EY8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EY8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ey8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EY8 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5958&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACHE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ey8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ey8 OCA], [https://pdbe.org/4ey8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ey8 RCSB], [https://www.ebi.ac.uk/pdbsum/4ey8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ey8 ProSAT]</span></td></tr>
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<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=4ey8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ey8 OCA], [http://pdbe.org/4ey8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ey8 RCSB], [http://www.ebi.ac.uk/pdbsum/4ey8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ey8 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ACES_HUMAN ACES_HUMAN]] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.<ref>PMID:2714437</ref> <ref>PMID:1748670</ref> <ref>PMID:1517212</ref> <ref>PMID:11985878</ref> [[http://www.uniprot.org/uniprot/TXFA2_DENAN TXFA2_DENAN]] This three-finger toxin selectively binds and inhibits with a 1:1 stoichiometry the mammalian and electric fish acetylcholinesterase (AChE) at picomolar concentrations. It is highly specific for the peripheral site on acetylcholinesterase. It has been called fasciculin since after injection into mice it cause severe, generalized and long-lasting (5-7 hours) fasciculations. The whole venom has anticoagulant activity, and the various components seem to act synergistically.
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[https://www.uniprot.org/uniprot/ACES_HUMAN ACES_HUMAN] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.<ref>PMID:2714437</ref> <ref>PMID:1748670</ref> <ref>PMID:1517212</ref> <ref>PMID:11985878</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human acetylcholinesterase (AChE) is a significant target for therapeutic drugs. Here we present high resolution crystal structures of human AChE, alone and in complexes with drug ligands; donepezil, an Alzheimer's disease drug, binds differently to human AChE than it does to Torpedo AChE. These crystals of human AChE provide a more accurate platform for further drug development than previously available.
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Structures of human acetylcholinesterase in complex with pharmacologically important ligands.,Cheung J, Rudolph MJ, Burshteyn F, Cassidy MS, Gary EN, Love J, Franklin MC, Height JJ J Med Chem. 2012 Oct 4. PMID:23035744<ref>PMID:23035744</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4ey8" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Acetylcholinesterase|Acetylcholinesterase]]
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*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
*[[Fasciculin|Fasciculin]]
*[[Fasciculin|Fasciculin]]
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*[[3D structures of acetylcholinesterase|3D structures of acetylcholinesterase]]
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acetylcholinesterase]]
 
[[Category: Dendroaspis angusticeps]]
[[Category: Dendroaspis angusticeps]]
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Burshteyn, F]]
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[[Category: Large Structures]]
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[[Category: Cassidy, M]]
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[[Category: Burshteyn F]]
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[[Category: Cheung, J]]
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[[Category: Cassidy M]]
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[[Category: Franklin, M]]
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[[Category: Cheung J]]
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[[Category: Gary, E]]
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[[Category: Franklin M]]
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[[Category: Height, J]]
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[[Category: Gary E]]
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[[Category: Love, J]]
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[[Category: Height J]]
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[[Category: Rudolph, M]]
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[[Category: Love J]]
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[[Category: Fasciculin 2]]
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[[Category: Rudolph M]]
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[[Category: Hydrolase]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Inhibitor]]
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[[Category: Snake venom toxin]]
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Current revision

Crystal structure of recombinant human acetylcholinesterase in complex with fasciculin-2

PDB ID 4ey8

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