2cek

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{{STRUCTURE_2cek| PDB=2cek | SCENE= }}
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==CONFORMATIONAL FLEXIBILITY IN THE PERIPHERAL SITE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE REVEALED BY THE COMPLEX STRUCTURE WITH A BIFUNCTIONAL INHIBITOR==
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===CONFORMATIONAL FLEXIBILITY IN THE PERIPHERAL SITE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE REVEALED BY THE COMPLEX STRUCTURE WITH A BIFUNCTIONAL INHIBITOR===
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<StructureSection load='2cek' size='340' side='right' caption='[[2cek]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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{{ABSTRACT_PUBMED_16594661}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2cek]] 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=2CEK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CEK FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[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]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cek OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cek RCSB], [http://www.ebi.ac.uk/pdbsum/2cek PDBsum]</span></td></tr>
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<table>
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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/ce/2cek_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata 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 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.
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==About this Structure==
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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>
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[[2cek]] 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=2CEK OCA].
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
==See Also==
==See Also==
*[[Acetylcholinesterase|Acetylcholinesterase]]
*[[Acetylcholinesterase|Acetylcholinesterase]]
*[[Torpedo californica acetylcholinesterase with bifunctional inhibitor|Torpedo californica acetylcholinesterase with bifunctional inhibitor]]
*[[Torpedo californica acetylcholinesterase with bifunctional inhibitor|Torpedo californica acetylcholinesterase with bifunctional inhibitor]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:016594661</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Acetylcholinesterase]]
[[Category: Acetylcholinesterase]]
[[Category: Torpedo californica]]
[[Category: Torpedo californica]]

Revision as of 01:24, 30 September 2014

CONFORMATIONAL FLEXIBILITY IN THE PERIPHERAL SITE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE REVEALED BY THE COMPLEX STRUCTURE WITH A BIFUNCTIONAL INHIBITOR

2cek, resolution 2.20Å

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