1vot
From Proteopedia
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| - | [[ | + | ==ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH HUPERZINE A== |
| + | <StructureSection load='1vot' size='340' side='right' caption='[[1vot]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1vot]] 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=1VOT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VOT FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HUP:HUPERZINE+A'>HUP</scene></td></tr> | ||
| + | <tr id='activity'><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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vot OCA], [http://pdbe.org/1vot PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vot RCSB], [http://www.ebi.ac.uk/pdbsum/1vot PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vo/1vot_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1vot ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | (-)-Huperzine A (HupA) is found in an extract from a club moss that has been used for centuries in Chinese folk medicine. Its action has been attributed to its ability to strongly inhibit acetylcholinesterase (AChE). The crystal structure of the complex of AChE with optically pure HupA at 2.5 A resolution shows an unexpected orientation for the inhibitor with surprisingly few strong direct interactions with protein residues to explain its high affinity. This structure is compared to the native structure of AChE devoid of any inhibitor as determined to the same resolution. An analysis of the affinities of structural analogues of HupA, correlated with their interactions with the protein, shows the importance of individual hydrophobic interactions between HupA and aromatic residues in the active-site gorge of AChE. | ||
| - | + | Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A.,Raves ML, Harel M, Pang YP, Silman I, Kozikowski AP, Sussman JL Nat Struct Biol. 1997 Jan;4(1):57-63. PMID:8989325<ref>PMID:8989325</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1vot" style="background-color:#fffaf0;"></div> | |
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==See Also== | ==See Also== | ||
*[[AChE inhibitors and substrates|AChE inhibitors and substrates]] | *[[AChE inhibitors and substrates|AChE inhibitors and substrates]] | ||
| - | *[[AChE inhibitors and substrates (Part II)|AChE inhibitors and substrates (Part II)]] | ||
*[[Acetylcholinesterase|Acetylcholinesterase]] | *[[Acetylcholinesterase|Acetylcholinesterase]] | ||
| - | *[[Alzheimer's Disease|Alzheimer's Disease]] | ||
*[[Huperzine A Complexed with Acetylcholinesterase|Huperzine A Complexed with Acetylcholinesterase]] | *[[Huperzine A Complexed with Acetylcholinesterase|Huperzine A Complexed with Acetylcholinesterase]] | ||
| + | *[[PDB identification code|PDB identification code]] | ||
| + | *[[3D structures of acetylcholinesterase|3D structures of acetylcholinesterase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[en:1vot]] | ||
| + | [[zh:1vot (Chinese)]] | ||
| - | ==Reference== | ||
| - | <ref group="xtra">PMID:008989325</ref><references group="xtra"/> | ||
[[Category: Acetylcholinesterase]] | [[Category: Acetylcholinesterase]] | ||
[[Category: Torpedo californica]] | [[Category: Torpedo californica]] | ||
| - | [[Category: Harel, M | + | [[Category: Harel, M]] |
| - | [[Category: Raves, M L | + | [[Category: Raves, M L]] |
| - | [[Category: Silman, I | + | [[Category: Silman, I]] |
| - | [[Category: Sussman, J L | + | [[Category: Sussman, J L]] |
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Neurotransmitter cleavage]] | [[Category: Neurotransmitter cleavage]] | ||
Current revision
ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH HUPERZINE A
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