1vzj

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<StructureSection load='1vzj' size='340' side='right'caption='[[1vzj]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='1vzj' size='340' side='right'caption='[[1vzj]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1vzj]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VZJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1vzj]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VZJ FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.35&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1b41|1b41]], [[1f8u|1f8u]], [[2clj|2clj]]</div></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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [https://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=1vzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzj OCA], [https://pdbe.org/1vzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vzj RCSB], [https://www.ebi.ac.uk/pdbsum/1vzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vzj ProSAT]</span></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=1vzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzj OCA], [https://pdbe.org/1vzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vzj RCSB], [https://www.ebi.ac.uk/pdbsum/1vzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vzj ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
 
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[[https://www.uniprot.org/uniprot/COLQ_HUMAN COLQ_HUMAN]] Defects in COLQ are the cause of congenital myasthenic syndrome Engel type (CMSE) [MIM:[https://omim.org/entry/603034 603034]]; also known as end-plate acetylcholinesterase deficiency or congenital myasthenic syndrome type IC (CMS-IC). CMSE is a rare autosomal recessive congenital myasthenic syndrome characterized by onset during childhood, generalized weakness, abnormal fatigability on exertion, refrectoriness to acetylcholinesterase drugs, decremental electromyographic response and morphological abnormalities of the neuromuscular junctions.<ref>PMID:9758617</ref> <ref>PMID:10665486</ref>
 
== Function ==
== Function ==
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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> [[https://www.uniprot.org/uniprot/COLQ_HUMAN COLQ_HUMAN]] Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.
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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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acetylcholinesterase]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bon, S]]
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[[Category: Bon S]]
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[[Category: Dvir, H]]
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[[Category: Dvir H]]
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[[Category: Garbay, C]]
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[[Category: Garbay C]]
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[[Category: Harel, M]]
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[[Category: Harel M]]
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[[Category: Liu, W Q]]
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[[Category: Liu W-Q]]
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[[Category: Massoulie, J]]
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[[Category: Massoulie J]]
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[[Category: Silman, I]]
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[[Category: Silman I]]
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[[Category: Sussman, J L]]
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[[Category: Sussman JL]]
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[[Category: Vidal, M]]
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[[Category: Vidal M]]
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[[Category: Alternative splicing]]
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[[Category: Disease mutation]]
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[[Category: Hydrolase]]
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[[Category: Neurotransmitter degradation]]
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[[Category: Synapse]]
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Revision as of 13:28, 9 May 2024

Structure of the tetramerization domain of acetylcholinesterase: four-fold interaction of a WWW motif with a left-handed polyproline helix

PDB ID 1vzj

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