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2cek
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Conformational Flexibility in the Peripheral Site of Torpedo californica Acetylcholinesterase Revealed by the Complex Structure with a Bifunctional Inhibitor== |
| - | <StructureSection load='2cek' size='340' side='right'caption='[[2cek]]' scene=''> | + | <StructureSection load='2cek' size='340' side='right'caption='[[2cek]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2cek]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CEK FirstGlance]. <br> |
| - | </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=2cek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cek OCA], [https://pdbe.org/2cek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cek RCSB], [https://www.ebi.ac.uk/pdbsum/2cek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cek ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=N8T:N-[8-(1,2,3,4-TETRAHYDROACRIDIN-9-YLTHIO)OCTYL]-1,2,3,4-TETRAHYDROACRIDIN-9-AMINE'>N8T</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1acj|1acj]], [[1acl|1acl]], [[1amn|1amn]], [[1ax9|1ax9]], [[1cfj|1cfj]], [[1dx6|1dx6]], [[1e3q|1e3q]], [[1e66|1e66]], [[1ea5|1ea5]], [[1eea|1eea]], [[1eve|1eve]], [[1fss|1fss]], [[1gpk|1gpk]], [[1gpn|1gpn]], [[1gqr|1gqr]], [[1gqs|1gqs]], [[1h22|1h22]], [[1h23|1h23]], [[1hbj|1hbj]], [[1jga|1jga]], [[1jgb|1jgb]], [[1jjb|1jjb]], [[1oce|1oce]], [[1odc|1odc]], [[1qid|1qid]], [[1qie|1qie]], [[1qif|1qif]], [[1qig|1qig]], [[1qih|1qih]], [[1qii|1qii]], [[1qij|1qij]], [[1qik|1qik]], [[1qim|1qim]], [[1qti|1qti]], [[1som|1som]], [[1u65|1u65]], [[1ut6|1ut6]], [[1vot|1vot]], [[1vxo|1vxo]], [[1vxr|1vxr]], [[1w4l|1w4l]], [[1w6r|1w6r]], [[1w75|1w75]], [[1w76|1w76]], [[1zgb|1zgb]], [[1zgc|1zgc]], [[2ace|2ace]], [[2ack|2ack]], [[2c4h|2c4h]], [[2c58|2c58]], [[2c5f|2c5f]], [[2c5g|2c5g]], [[2dfp|2dfp]], [[3ace|3ace]], [[4ace|4ace]]</div></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] </span></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=2cek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cek OCA], [https://pdbe.org/2cek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cek RCSB], [https://www.ebi.ac.uk/pdbsum/2cek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cek ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/ACES_TORCA ACES_TORCA]] 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=2cek ConSurf]. | </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=2cek ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The X-ray crystallographic structure of Torpedo californica acetylcholinesterase (TcAChE) in complex with the bifunctional inhibitor NF595, a potentially new anti-Alzheimer drug, has been solved. For the first time in TcAChE, a major conformational change in the peripheral-site tryptophan residue is observed upon complexation. The observed conformational flexibility highlights the dynamic nature of protein structures and is of importance for structure-based drug design. | ||
| + | |||
| + | Conformational flexibility in the peripheral site of Torpedo californica acetylcholinesterase revealed by the complex structure with a bifunctional inhibitor.,Colletier JP, Sanson B, Nachon F, Gabellieri E, Fattorusso C, Campiani G, Weik M J Am Chem Soc. 2006 Apr 12;128(14):4526-7. PMID:16594661<ref>PMID:16594661</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2cek" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Acetylcholinesterase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Torpedo californica]] |
| + | [[Category: Campiani, G]] | ||
| + | [[Category: Colletier, J P]] | ||
| + | [[Category: Fattorusso, C]] | ||
| + | [[Category: Gabellieri, E]] | ||
| + | [[Category: Nachon, F]] | ||
| + | [[Category: Sanson, B]] | ||
| + | [[Category: Weik, M]] | ||
| + | [[Category: Alpha/beta hydrolase]] | ||
| + | [[Category: Alternative splicing]] | ||
| + | [[Category: Alzheimer disease]] | ||
| + | [[Category: Conformational flexibility]] | ||
| + | [[Category: Glycoprotein]] | ||
| + | [[Category: Gpi-anchor]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Lipoprotein]] | ||
| + | [[Category: Neurotransmitter cleavage]] | ||
| + | [[Category: Neurotransmitter degradation]] | ||
| + | [[Category: Serine esterase]] | ||
| + | [[Category: Synapse]] | ||
| + | [[Category: Synapse membrane]] | ||
Revision as of 09:17, 24 February 2021
Conformational Flexibility in the Peripheral Site of Torpedo californica Acetylcholinesterase Revealed by the Complex Structure with a Bifunctional Inhibitor
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Categories: Acetylcholinesterase | Large Structures | Torpedo californica | Campiani, G | Colletier, J P | Fattorusso, C | Gabellieri, E | Nachon, F | Sanson, B | Weik, M | Alpha/beta hydrolase | Alternative splicing | Alzheimer disease | Conformational flexibility | Glycoprotein | Gpi-anchor | Hydrolase | Lipoprotein | Neurotransmitter cleavage | Neurotransmitter degradation | Serine esterase | Synapse | Synapse membrane
