1w75

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[[Image:1w75.gif|left|200px]]
 
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{{Structure
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==Native Orthorhombic form of Torpedo californica acetylcholinesterase (AChE)==
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|PDB= 1w75 |SIZE=350|CAPTION= <scene name='initialview01'>1w75</scene>, resolution 2.400&Aring;
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<StructureSection load='1w75' size='340' side='right'caption='[[1w75]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+B'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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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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|ACTIVITY= [http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7]
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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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|GENE=
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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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}}
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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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'''NATIVE ORTHORHOMBIC FORM OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE (ACHE)'''
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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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==Overview==
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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 ==
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.
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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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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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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==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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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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</div>
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[[Category: Acetylcholinesterase]]
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<div class="pdbe-citations 1w75" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Torpedo californica]]
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[[Category: Argaman, A.]]
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[[Category: Botti, S.]]
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[[Category: Greenblatt, H M.]]
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[[Category: Silman, I.]]
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[[Category: Sussman, J L.]]
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[[Category: NAG]]
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[[Category: alzheimer's disease]]
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[[Category: cholinesterase]]
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[[Category: glycoprotein]]
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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 Thu Mar 20 14:53:04 2008''
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==See Also==
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*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Tetronarce californica]]
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[[Category: Argaman A]]
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[[Category: Botti S]]
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[[Category: Greenblatt HM]]
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[[Category: Silman I]]
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[[Category: Sussman JL]]

Current revision

Native Orthorhombic form of Torpedo californica acetylcholinesterase (AChE)

PDB ID 1w75

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