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3zv7

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Revision as of 15:42, 5 August 2016

Torpedo californica Acetylcholinesterase Inhibition by Bisnorcymserine

Structural highlights

3zv7 is a 1 chain structure with sequence from Torpedo californica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , ,
Related:	1zgb, 1qti, 1amn, 1e66, 2vq6, 2ack, 2j3d, 1qii, 2ckm, 1dx6, 1qie, 1qij, 1acl, 1odc, 1w4l, 2cmf, 2wg0, 2j3q, 1gqs, 2j4f, 1e3q, 1qik, 2dfp, 2c5f, 1ea5, 1qif, 2vjc, 1eea, 2vjb, 1qig, 1qid, 1zgc, 2wfz, 2vjd, 1jjb, 2wg1, 1ut6, 2vt6, 2wg2, 2w9i, 2vt7, 2cek, 1qim, 1jga, 1gpk, 3ace, 1oce, 1w6r, 1som, 1vxo, 2vja, 2w6c, 1cfj, 2v96, 1ax9, 1w76, 1u65, 1h22, 1eve, 2c4h, 1gqr, 2va9, 2ace, 1vxr, 4ace, 2c58, 1hbj, 1w75, 1vot, 2c5g, 2v98, 1jgb, 2xi4, 1gpn, 1qih, 1h23, 1fss, 1acj, 2v97
Activity:	Acetylcholinesterase, with EC number 3.1.1.7
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.

Publication Abstract from PubMed

Natural and synthetic carbamates act as pseudo-irreversible inhibitors of AChE (acetylcholinesterase) as well as BChE (butyrylcholinesterase), two enzymes involved in neuronal function as well as in the development and progression of AD (Alzheimer's disease). The AChE mode of action is characterized by a rapid carbamoylation of the active-site Ser200 with release of a leaving group followed by a slow regeneration of enzyme action due to subsequent decarbamoylation. The experimental AD therapeutic bisnorcymserine, a synthetic carbamate, shows an interesting activity and selectivity for BChE, and its clinical development is currently being pursued. We undertook detailed kinetic studies on the activity of the carbamate bisnorcymserine with Tc (Torpedo californica) AChE and, on the basis of the results, crystallized the complex between TcAChE and bisnorcymserine. The X-ray crystal structure showed only the leaving group, bisnoreseroline, trapped at the bottom of the aromatic enzyme gorge. Specifically, bisnoreseroline interacts in a non-covalent way with Ser200 and His440, disrupting the existing interactions within the catalytic triad, and it stacks with Trp84 at the bottom of the gorge, giving rise to an unprecedented hydrogen-bonding contact. These interactions point to a dominant reversible inhibition mechanism attributable to the leaving group, bisnoreseroline, as revealed by kinetic analysis.

Kinetics of Torpedo californica acetylcholinesterase inhibition by bisnorcymserine and crystal structure of the complex with its leaving group.,Bartolucci C, Stojan J, Yu QS, Greig NH, Lamba D Biochem J. 2012 Jun 1;444(2):269-77. PMID:22390827^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bartolucci C, Stojan J, Yu QS, Greig NH, Lamba D. Kinetics of Torpedo californica acetylcholinesterase inhibition by bisnorcymserine and crystal structure of the complex with its leaving group. Biochem J. 2012 Jun 1;444(2):269-77. PMID:22390827 doi:10.1042/BJ20111675

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3zv7"

@@ Line 1: / Line 1: @@
 ==Torpedo californica Acetylcholinesterase Inhibition by Bisnorcymserine==
 <StructureSection load='3zv7' size='340' side='right' caption='[[3zv7]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zgb|1zgb]], [[1qti|1qti]], [[1amn|1amn]], [[1e66|1e66]], [[2vq6|2vq6]], [[2ack|2ack]], [[2j3d|2j3d]], [[1qii|1qii]], [[2ckm|2ckm]], [[1dx6|1dx6]], [[1qie|1qie]], [[1qij|1qij]], [[1acl|1acl]], [[1odc|1odc]], [[1w4l|1w4l]], [[2cmf|2cmf]], [[2wg0|2wg0]], [[2j3q|2j3q]], [[1gqs|1gqs]], [[2j4f|2j4f]], [[1e3q|1e3q]], [[1qik|1qik]], [[2dfp|2dfp]], [[2c5f|2c5f]], [[1ea5|1ea5]], [[1qif|1qif]], [[2vjc|2vjc]], [[1eea|1eea]], [[2vjb|2vjb]], [[1qig|1qig]], [[1qid|1qid]], [[1zgc|1zgc]], [[2wfz|2wfz]], [[2vjd|2vjd]], [[1jjb|1jjb]], [[2wg1|2wg1]], [[1ut6|1ut6]], [[2vt6|2vt6]], [[2wg2|2wg2]], [[2w9i|2w9i]], [[2vt7|2vt7]], [[2cek|2cek]], [[1qim|1qim]], [[1jga|1jga]], [[1gpk|1gpk]], [[3ace|3ace]], [[1oce|1oce]], [[1w6r|1w6r]], [[1som|1som]], [[1vxo|1vxo]], [[2vja|2vja]], [[2w6c|2w6c]], [[1cfj|1cfj]], [[2v96|2v96]], [[1ax9|1ax9]], [[1w76|1w76]], [[1u65|1u65]], [[1h22|1h22]], [[1eve|1eve]], [[2c4h|2c4h]], [[1gqr|1gqr]], [[2va9|2va9]], [[2ace|2ace]], [[1vxr|1vxr]], [[4ace|4ace]], [[2c58|2c58]], [[1hbj|1hbj]], [[1w75|1w75]], [[1vot|1vot]], [[2c5g|2c5g]], [[2v98|2v98]], [[1jgb|1jgb]], [[2xi4|2xi4]], [[1gpn|1gpn]], [[1qih|1qih]], [[1h23|1h23]], [[1fss|1fss]], [[1acj|1acj]], [[2v97|2v97]]</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=3zv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zv7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zv7 RCSB], [http://www.ebi.ac.uk/pdbsum/3zv7 PDBsum]</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=3zv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zv7 OCA], [http://pdbe.org/3zv7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zv7 RCSB], [http://www.ebi.ac.uk/pdbsum/3zv7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zv7 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3zv7" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Acetylcholinesterase|Acetylcholinesterase]]
+*[[3D structures of acetylcholinesterase|3D structures of acetylcholinesterase]]
 == References ==
 <references/>

3zv7

From Proteopedia

Revision as of 15:42, 5 August 2016

Torpedo californica Acetylcholinesterase Inhibition by Bisnorcymserine

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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