1qti

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{{STRUCTURE_1qti| PDB=1qti | SCENE= }}
 
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===Acetylcholinesterase (E.C.3.1.1.7)===
 
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{{ABSTRACT_PUBMED_11119642}}
 
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==About this Structure==
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==Acetylcholinesterase (E.C.3.1.1.7)==
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[[1qti]] is a 1 chain structure 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=1QTI OCA].
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<StructureSection load='1qti' size='340' side='right'caption='[[1qti]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 2.5&#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=GNT:(-)-GALANTHAMINE'>GNT</scene></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=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>
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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/qt/1qti_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=1qti 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 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.
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==See Also==
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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>
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*[[AChE inhibitors and substrates|AChE inhibitors and substrates]]
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*[[Acetylcholinesterase|Acetylcholinesterase]]
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:011119642</ref><references group="xtra"/>
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</div>
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[[Category: Acetylcholinesterase]]
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<div class="pdbe-citations 1qti" style="background-color:#fffaf0;"></div>
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[[Category: Torpedo californica]]
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[[Category: Bartolucci, C.]]
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==See Also==
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[[Category: Fels, G.]]
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*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
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[[Category: Lamba, D.]]
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== References ==
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[[Category: Perola, E.]]
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<references/>
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[[Category: Pilger, C.]]
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__TOC__
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[[Category: Alpha/beta hydrolase]]
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</StructureSection>
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[[Category: Alzheimer's disease]]
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[[Category: Large Structures]]
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[[Category: Catalytic triad]]
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[[Category: Tetronarce californica]]
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[[Category: Drug]]
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[[Category: Bartolucci C]]
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[[Category: Hydrolase]]
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[[Category: Fels G]]
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[[Category: Neurotransmitter cleaveage]]
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[[Category: Lamba D]]
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[[Category: Serine hydrolase]]
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[[Category: Perola E]]
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[[Category: Pilger C]]

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Acetylcholinesterase (E.C.3.1.1.7)

PDB ID 1qti

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