1w75

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[[Image:1w75.gif|left|200px]]
 
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==Native Orthorhombic form of Torpedo californica acetylcholinesterase (AChE)==
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The line below this paragraph, containing "STRUCTURE_1w75", creates the "Structure Box" on the page.
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<StructureSection load='1w75' size='340' side='right'caption='[[1w75]], [[Resolution|resolution]] 2.40&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'>[[1w75]] is a 2 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=1W75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W75 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]] 2.4&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_1w75| PDB=1w75 | 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=1w75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w75 OCA], [https://pdbe.org/1w75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w75 RCSB], [https://www.ebi.ac.uk/pdbsum/1w75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w75 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/w7/1w75_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=1w75 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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Bifunctional derivatives of the alkaloid galanthamine, designed to interact with both the active site of the enzyme acetylcholinesterase (AChE) and its peripheral cation binding site, have been assayed with Torpedo californica AChE (TcAChE), and the three-dimensional structures of their complexes with the enzyme have been solved by X-ray crystallography. Differences were noted between the IC(50) values obtained for TcAChE and those for Electrophorus electricus AChE. These differences are ascribed to sequence differences in one or two residues lining the active-site gorge of the enzyme. The binding of one of the inhibitors disrupts the native conformation of one wall of the gorge, formed by the loop Trp279-Phe290. It is proposed that flexibility of this loop may permit the binding of inhibitors such as galanthamine, which are too bulky to penetrate the narrow neck of the gorge formed by Tyr121 and Phe330 as seen in the crystal structure.
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'''NATIVE ORTHORHOMBIC FORM OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE (ACHE)'''
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The complex of a bivalent derivative of galanthamine with torpedo acetylcholinesterase displays drastic deformation of the active-site gorge: implications for structure-based drug design.,Greenblatt HM, Guillou C, Guenard D, Argaman A, Botti S, Badet B, Thal C, Silman I, Sussman JL J Am Chem Soc. 2004 Dec 1;126(47):15405-11. PMID:15563167<ref>PMID:15563167</ref>
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==Overview==
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Bifunctional derivatives of the alkaloid galanthamine, designed to interact with both the active site of the enzyme acetylcholinesterase (AChE) and its peripheral cation binding site, have been assayed with Torpedo californica AChE (TcAChE), and the three-dimensional structures of their complexes with the enzyme have been solved by X-ray crystallography. Differences were noted between the IC(50) values obtained for TcAChE and those for Electrophorus electricus AChE. These differences are ascribed to sequence differences in one or two residues lining the active-site gorge of the enzyme. The binding of one of the inhibitors disrupts the native conformation of one wall of the gorge, formed by the loop Trp279-Phe290. It is proposed that flexibility of this loop may permit the binding of inhibitors such as galanthamine, which are too bulky to penetrate the narrow neck of the gorge formed by Tyr121 and Phe330 as seen in the crystal structure.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1W75 is a [[Single protein]] structure of 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=1W75 OCA].
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</div>
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<div class="pdbe-citations 1w75" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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The complex of a bivalent derivative of galanthamine with torpedo acetylcholinesterase displays drastic deformation of the active-site gorge: implications for structure-based drug design., Greenblatt HM, Guillou C, Guenard D, Argaman A, Botti S, Badet B, Thal C, Silman I, Sussman JL, J Am Chem Soc. 2004 Dec 1;126(47):15405-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15563167 15563167]
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*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
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[[Category: Acetylcholinesterase]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Torpedo californica]]
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__TOC__
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[[Category: Argaman, A.]]
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</StructureSection>
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[[Category: Botti, S.]]
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[[Category: Large Structures]]
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[[Category: Greenblatt, H M.]]
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[[Category: Tetronarce californica]]
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[[Category: Silman, I.]]
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[[Category: Argaman A]]
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[[Category: Sussman, J L.]]
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[[Category: Botti S]]
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[[Category: Alzheimer's disease]]
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[[Category: Greenblatt HM]]
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[[Category: Cholinesterase]]
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[[Category: Silman I]]
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[[Category: Glycoprotein]]
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[[Category: Sussman JL]]
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[[Category: Gpi-anchor]]
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[[Category: Hydrolase]]
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[[Category: Muscle]]
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[[Category: Nerve]]
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[[Category: Neurotransmitter degradation]]
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[[Category: Serine esterase]]
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[[Category: Serine hydrolase]]
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[[Category: Signal]]
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[[Category: Synapse]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:14:57 2008''
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Current revision

Native Orthorhombic form of Torpedo californica acetylcholinesterase (AChE)

PDB ID 1w75

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