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1dx6

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Revision as of 02:55, 11 September 2015

STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH (-)-GALANTHAMINE AT 2.3A RESOLUTION

Structural highlights

1dx6 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:	2ace, 3ace, 4ace, 1acj, 2ack, 1acl, 1amn, 1fss, 1vot, 1ax9, 1eve, 1cfj
Activity:	Acetylcholinesterase, with EC number 3.1.1.7
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

(-)-Galanthamine (GAL), an alkaloid from the flower, the common snowdrop (Galanthus nivalis), shows anticholinesterase activity. This property has made GAL the target of research as to its effectiveness in the treatment of Alzheimer's disease. We have solved the X-ray crystal structure of GAL bound in the active site of Torpedo californica acetylcholinesterase (TcAChE) to 2.3 A resolution. The inhibitor binds at the base of the active site gorge of TcAChE, interacting with both the choline-binding site (Trp-84) and the acyl-binding pocket (Phe-288, Phe-290). The tertiary amine group of GAL does not interact closely with Trp-84; rather, the double bond of its cyclohexene ring stacks against the indole ring. The tertiary amine appears to make a non-conventional hydrogen bond, via its N-methyl group, to Asp-72, near the top of the gorge. The hydroxyl group of the inhibitor makes a strong hydrogen bond (2.7 A) with Glu-199. The relatively tight binding of GAL to TcAChE appears to arise from a number of moderate to weak interactions with the protein, coupled to a low entropy cost for binding due to the rigid nature of the inhibitor.

Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3 A resolution.,Greenblatt HM, Kryger G, Lewis T, Silman I, Sussman JL FEBS Lett. 1999 Dec 17;463(3):321-6. PMID:10606746^[1]

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

References

↑ Greenblatt HM, Kryger G, Lewis T, Silman I, Sussman JL. Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3 A resolution. FEBS Lett. 1999 Dec 17;463(3):321-6. PMID:10606746

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dx6"

@@ Line 6: / Line 6: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ace|2ace]], [[3ace|3ace]], [[4ace|4ace]], [[1acj|1acj]], [[2ack|2ack]], [[1acl|1acl]], [[1amn|1amn]], [[1fss|1fss]], [[1vot|1vot]], [[1ax9|1ax9]], [[1eve|1eve]], [[1cfj|1cfj]]</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=1dx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dx6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dx6 RCSB], [http://www.ebi.ac.uk/pdbsum/1dx6 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=1dx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dx6 OCA], [http://pdbe.org/1dx6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dx6 RCSB], [http://www.ebi.ac.uk/pdbsum/1dx6 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1dx6" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[AChE bivalent inhibitors (Part II)|AChE bivalent inhibitors (Part II)]]
 *[[AChE inhibitors and substrates|AChE inhibitors and substrates]]
-*[[AChE inhibitors and substrates (Part II)|AChE inhibitors and substrates (Part II)]]
-*[[AChE inhibitors and substrates (Part III)|AChE inhibitors and substrates (Part III)]]
 *[[Acetylcholinesterase|Acetylcholinesterase]]
 *[[Complex of TcAChE with an iminium galanthamine derivative|Complex of TcAChE with an iminium galanthamine derivative]]

1dx6

From Proteopedia

Revision as of 02:55, 11 September 2015

STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH (-)-GALANTHAMINE AT 2.3A RESOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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