4ey8: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 4ey8 is ON HOLD
+==Crystal structure of recombinant human acetylcholinesterase in complex with fasciculin-2==
+<StructureSection load='4ey8' size='340' side='right'caption='[[4ey8]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+<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>
+</table>
+== Function ==
+[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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-Authors: Cheung, J., Rudolph, M., Burshteyn, F., Cassidy, M., Gary, E., Love, J., Height, J., Franklin, M.
+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>
-Description: Crystal structure of recombinant human acetylcholinesterase in complex with fasciculin-2
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4ey8" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
+*[[Fasciculin|Fasciculin]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Dendroaspis angusticeps]]
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Burshteyn F]]
+[[Category: Cassidy M]]
+[[Category: Cheung J]]
+[[Category: Franklin M]]
+[[Category: Gary E]]
+[[Category: Height J]]
+[[Category: Love J]]
+[[Category: Rudolph M]]