1qti
From Proteopedia
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- | {{STRUCTURE_1qti| PDB=1qti | SCENE= }} | ||
- | ===Acetylcholinesterase (E.C.3.1.1.7)=== | ||
- | {{ABSTRACT_PUBMED_11119642}} | ||
- | == | + | ==Acetylcholinesterase (E.C.3.1.1.7)== |
- | [[1qti]] is a 1 chain structure with sequence from [ | + | <StructureSection load='1qti' size='340' side='right'caption='[[1qti]], [[Resolution|resolution]] 2.50Å' scene=''> |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1qti]] 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=1QTI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QTI 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]] 2.5Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNT:(-)-GALANTHAMINE'>GNT</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=1qti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qti OCA], [https://pdbe.org/1qti PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qti RCSB], [https://www.ebi.ac.uk/pdbsum/1qti PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qti ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [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. | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qt/1qti_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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=1qti ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The 3D structure of a complex of the anti-Alzheimer drug galanthamine with Torpedo californica acetylcholinesterase is reported. Galanthamine, a tertiary alkaloid extracted from several species of Amarylidacae, is so far the only drug that shows a dual activity, being both an acetylcholinesterase inhibitor and an allosteric potentiator of the nicotinic response induced by acetylcholine and competitive agonists. The X-ray structure, at 2.5A resolution, shows an unexpected orientation of the ligand within the active site, as well as unusual protein-ligand interactions. The inhibitor binds at the base of the active site gorge, interacting with both the acyl-binding pocket and the principal quaternary ammonium-binding site. However, the tertiary amine group of galanthamine does not directly interact with Trp84. A docking study using the program AUTODOCK correctly predicts the orientation of galanthamine in the active site. The docked lowest-energy structure has a root mean square deviation of 0.5A with respect to the corresponding crystal structure of the complex. The observed binding mode explains the affinities of a series of structural analogs of galanthamine and provides a rational basis for structure-based drug design of synthetic derivatives with improved pharmacological properties. Proteins 2001;42:182-191. | ||
- | + | Three-dimensional structure of a complex of galanthamine (Nivalin) with acetylcholinesterase from Torpedo californica: implications for the design of new anti-Alzheimer drugs.,Bartolucci C, Perola E, Pilger C, Fels G, Lamba D Proteins. 2001 Feb 1;42(2):182-91. PMID:11119642<ref>PMID:11119642</ref> | |
- | + | ||
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | < | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 1qti" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | |
- | [[Category: Bartolucci | + | ==See Also== |
- | [[Category: Fels | + | *[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]] |
- | [[Category: Lamba | + | == References == |
- | [[Category: Perola | + | <references/> |
- | [[Category: Pilger | + | __TOC__ |
- | + | </StructureSection> | |
- | + | [[Category: Large Structures]] | |
- | + | [[Category: Tetronarce californica]] | |
- | + | [[Category: Bartolucci C]] | |
- | + | [[Category: Fels G]] | |
- | + | [[Category: Lamba D]] | |
- | + | [[Category: Perola E]] | |
+ | [[Category: Pilger C]] |
Current revision
Acetylcholinesterase (E.C.3.1.1.7)
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