1ut6

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[[Image:1ut6.png|left|200px]]
 
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==Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with N-9-(1',2',3',4'-Tetrahydroacridinyl)-1,8- diaminooctane at 2.4 angstroms resolution.==
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The line below this paragraph, containing "STRUCTURE_1ut6", creates the "Structure Box" on the page.
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<StructureSection load='1ut6' size='340' side='right'caption='[[1ut6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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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'>[[1ut6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetronarce_californica Tetronarce californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UT6 FirstGlance]. <br>
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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]] 2.4&#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=A8N:N-9-(1,2,3,4-TETRAHYDROACRIDINYL)-1,8-DIAMINOOCTANE'>A8N</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_1ut6| PDB=1ut6 | 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=1ut6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ut6 OCA], [https://pdbe.org/1ut6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ut6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ut6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ut6 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACES_TETCF ACES_TETCF] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.
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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/ut/1ut6_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=1ut6 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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The X-ray crystal structures were solved for complexes with Torpedo californica acetylcholinesterase of two bivalent tacrine derivative compounds in which the two tacrine rings were separated by 5- and 7-carbon spacers. The derivative with the 7-carbon spacer spans the length of the active-site gorge, making sandwich interactions with aromatic residues both in the catalytic anionic site (Trp84 and Phe330) at the bottom of the gorge and at the peripheral anionic site near its mouth (Tyr70 and Trp279). The derivative with the 5-carbon spacer interacts in a similar manner at the bottom of the gorge, but the shorter tether precludes a sandwich interaction at the peripheral anionic site. Although the upper tacrine group does interact with Trp279, it displaces the phenyl residue of Phe331, thus causing a major rearrangement in the Trp279-Ser291 loop. The ability of this inhibitor to induce large-scale structural changes in the active-site gorge of acetylcholinesterase has significant implications for structure-based drug design because such conformational changes in the target enzyme are difficult to predict and to model.
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===STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH N-9-(1',2',3',4'-TETRAHYDROACRIDINYL)-1,8-DIAMINOOCTANE AT 2.4 ANGSTROMS RESOLUTION.===
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Complexes of alkylene-linked tacrine dimers with Torpedo californica acetylcholinesterase: Binding of Bis5-tacrine produces a dramatic rearrangement in the active-site gorge.,Rydberg EH, Brumshtein B, Greenblatt HM, Wong DM, Shaya D, Williams LD, Carlier PR, Pang YP, Silman I, Sussman JL J Med Chem. 2006 Sep 7;49(18):5491-500. PMID:16942022<ref>PMID:16942022</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 class="pdbe-citations 1ut6" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16942022 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16942022}}
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==About this Structure==
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[[1ut6]] is a 1 chain structure of [[Acetylcholinesterase]] with sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UT6 OCA].
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==See Also==
==See Also==
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*[[AChE bivalent inhibitors|AChE bivalent inhibitors]]
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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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*[[Acetylcholinesterase complexed with N-9-(1'%2C2'%2C3'%2C4'-tetrahydroacridinyl)-1%2C8-diaminooctane|Acetylcholinesterase complexed with N-9-(1'%2C2'%2C3'%2C4'-tetrahydroacridinyl)-1%2C8-diaminooctane]]
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<references/>
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*[[Alzheimer's Disease|Alzheimer's Disease]]
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__TOC__
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*[[Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (5 carbon linker)|Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (5 carbon linker)]]
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</StructureSection>
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*[[Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (7 carbon linker)|Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (7 carbon linker)]]
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[[Category: Large Structures]]
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*[[User:Boris Brumshtein|User:Boris Brumshtein]]
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[[Category: Tetronarce californica]]
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*[[User:Dawn M. Wong|User:Dawn M. Wong]]
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[[Category: Brumshtein B]]
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[[Category: Carlier PR]]
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==Reference==
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[[Category: Greenblatt HM]]
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<ref group="xtra">PMID:016942022</ref><ref group="xtra">PMID:012517147</ref><ref group="xtra">PMID:010514292</ref><ref group="xtra">PMID:007738603</ref><ref group="xtra">PMID:008415649</ref><ref group="xtra">PMID:001678899</ref><references group="xtra"/>
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[[Category: Pang Y-P]]
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[[Category: Acetylcholinesterase]]
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[[Category: Silman I]]
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[[Category: Torpedo californica]]
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[[Category: Sussman JL]]
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[[Category: Brumshtein, B.]]
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[[Category: Wong DM]]
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[[Category: Carlier, P R.]]
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[[Category: Greenblatt, H M.]]
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[[Category: Pang, Y P.]]
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[[Category: Silman, I.]]
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[[Category: Sussman, J L.]]
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[[Category: Wong, D M.]]
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[[Category: Acetylcholinesterase]]
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[[Category: Alzheimer's disease]]
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[[Category: Amine]]
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[[Category: Bivalent ligand]]
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[[Category: Dual-site binding]]
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[[Category: Glycoprotein]]
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[[Category: Gpi-anchor neurotransmitter degradation]]
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[[Category: Heterodimer]]
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[[Category: Hydrolase]]
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[[Category: Inhibitor]]
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[[Category: Membrane]]
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[[Category: Muscle]]
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[[Category: Nerve]]
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[[Category: Neurotransmitter cleavage]]
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[[Category: Serine esterase synapse]]
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[[Category: Serine hydrolase]]
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[[Category: Tacrine]]
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Current revision

Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with N-9-(1',2',3',4'-Tetrahydroacridinyl)-1,8- diaminooctane at 2.4 angstroms resolution.

PDB ID 1ut6

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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