1vzj

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{{STRUCTURE_1vzj| PDB=1vzj | SCENE= }}
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==STRUCTURE OF THE TETRAMERIZATION DOMAIN OF ACETYLCHOLINESTERASE: FOUR-FOLD INTERACTION OF A WWW MOTIF WITH A LEFT-HANDED POLYPROLINE HELIX==
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===STRUCTURE OF THE TETRAMERIZATION DOMAIN OF ACETYLCHOLINESTERASE: FOUR-FOLD INTERACTION OF A WWW MOTIF WITH A LEFT-HANDED POLYPROLINE HELIX===
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<StructureSection load='1vzj' size='340' side='right' caption='[[1vzj]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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{{ABSTRACT_PUBMED_15526038}}
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== 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VZJ FirstGlance]. <br>
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</td></tr><tr><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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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b41|1b41]], [[1f8u|1f8u]], [[2clj|2clj]]</td></tr>
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<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1vzj RCSB], [http://www.ebi.ac.uk/pdbsum/1vzj PDBsum]</span></td></tr>
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<table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/COLQ_HUMAN COLQ_HUMAN]] Defects in COLQ are the cause of congenital myasthenic syndrome Engel type (CMSE) [MIM:[http://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>
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== 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/COLQ_HUMAN COLQ_HUMAN]] Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vz/1vzj_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Functional localization of acetylcholinesterase (AChE) in vertebrate muscle and brain depends on interaction of the tryptophan amphiphilic tetramerization (WAT) sequence, at the C-terminus of its major splice variant (T), with a proline-rich attachment domain (PRAD), of the anchoring proteins, collagenous (ColQ) and proline-rich membrane anchor. The crystal structure of the WAT/PRAD complex reveals a novel supercoil structure in which four parallel WAT chains form a left-handed superhelix around an antiparallel left-handed PRAD helix resembling polyproline II. The WAT coiled coils possess a WWW motif making repetitive hydrophobic stacking and hydrogen-bond interactions with the PRAD. The WAT chains are related by an approximately 4-fold screw axis around the PRAD. Each WAT makes similar but unique interactions, consistent with an asymmetric pattern of disulfide linkages between the AChE tetramer subunits and ColQ. The P59Q mutation in ColQ, which causes congenital endplate AChE deficiency, and is located within the PRAD, disrupts crucial WAT-WAT and WAT-PRAD interactions. A model is proposed for the synaptic AChE(T) tetramer.
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==Disease==
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The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix.,Dvir H, Harel M, Bon S, Liu WQ, Vidal M, Garbay C, Sussman JL, Massoulie J, Silman I EMBO J. 2004 Nov 10;23(22):4394-405. Epub 2004 Nov 4. PMID:15526038<ref>PMID:15526038</ref>
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[[http://www.uniprot.org/uniprot/COLQ_HUMAN COLQ_HUMAN]] Defects in COLQ are the cause of congenital myasthenic syndrome Engel type (CMSE) [MIM:[http://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>
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==Function==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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/COLQ_HUMAN COLQ_HUMAN]] Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.
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</div>
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==About this Structure==
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[[1vzj]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZJ OCA].
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==See Also==
==See Also==
*[[AChE inhibitors and substrates|AChE inhibitors and substrates]]
*[[AChE inhibitors and substrates|AChE inhibitors and substrates]]
*[[Acetylcholinesterase|Acetylcholinesterase]]
*[[Acetylcholinesterase|Acetylcholinesterase]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:015526038</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Acetylcholinesterase]]
[[Category: Acetylcholinesterase]]
[[Category: Bon, S.]]
[[Category: Bon, S.]]

Revision as of 20:29, 29 September 2014

STRUCTURE OF THE TETRAMERIZATION DOMAIN OF ACETYLCHOLINESTERASE: FOUR-FOLD INTERACTION OF A WWW MOTIF WITH A LEFT-HANDED POLYPROLINE HELIX

1vzj, resolution 2.35Å

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