1vzj

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[[Image:1vzj.png|left|200px]]
 
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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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The line below this paragraph, containing "STRUCTURE_1vzj", creates the "Structure Box" on the page.
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<StructureSection load='1vzj' size='340' side='right'caption='[[1vzj]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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='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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{{STRUCTURE_1vzj| PDB=1vzj | SCENE= }}
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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>
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</table>
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== 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>
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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/initialview03.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/main_output.php?pdb_ID=1vzj 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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===STRUCTURE OF THE TETRAMERIZATION DOMAIN OF ACETYLCHOLINESTERASE: FOUR-FOLD INTERACTION OF A WWW MOTIF WITH A LEFT-HANDED POLYPROLINE HELIX===
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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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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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The line below this paragraph, {{ABSTRACT_PUBMED_15526038}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1vzj" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15526038 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15526038}}
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==About this Structure==
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[[1vzj]] is a 10 chain structure of [[Acetylcholinesterase]]. 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==
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*[[AChE inhibitors and substrates|AChE inhibitors and substrates]]
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*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
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*[[Acetylcholinesterase|Acetylcholinesterase]]
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== References ==
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*[[Structure Gallery Generator|Structure Gallery Generator]]
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<references/>
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*[[Tetramerization domain of acetylcholinesterase|Tetramerization domain of acetylcholinesterase]]
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Homo sapiens]]
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<ref group="xtra">PMID:015526038</ref><references group="xtra"/>
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[[Category: Large Structures]]
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[[Category: Acetylcholinesterase]]
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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 JL]]
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[[Category: Sussman, J L.]]
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[[Category: Vidal M]]
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[[Category: Vidal, M.]]
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[[Category: Acetylcholinesterase]]
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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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Current revision

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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