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1e3q

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Revision as of 02:09, 11 September 2015

TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH BW284C51

Structural highlights

1e3q 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, 1oce, 2dfp, 1som, 2dx6, 1vxo, 1vxr, 1qti, 1qig, 1qih, 1qii, 1qij, 1qik, 1qim, 1qid, 1qie, 1qif, 1eea
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

The X-ray crystal structure of Torpedo californica acetylcholinesterase (TcAChE) complexed with BW284C51 [CO[-CH(2)CH(2)-pC(6)H(4)-N(CH(3))(2)(CH(2)-CH=CH(2))](2)] is described and compared with the complexes of two other active-site gorge-spanning inhibitors, decamethonium and E2020. The inhibitor was soaked into TcAChE crystals in the trigonal space group P3(1)21, yielding a complex which diffracted to 2.85 A resolution. The structure was refined to an R factor of 19.0% and an R(free) of 23.4%; the final model contains the protein, inhibitor, 132 water molecules and three carbohydrate moieties. BW284C51 binds similarly to decamethonium and E2020, with its two phenyl and quaternary amino end-groups complexed to Trp84 in the catalytic site and to Trp279 in the peripheral binding site, and its central carbonyl group hydrogen bonded very weakly to Tyr121. Possible reasons for decamethonium's weaker binding are considered. The relative strength of binding of bisquaternary inhibitors to acetylcholinesterase and the effect of several mutations of the enzyme are discussed in the context of the respective X-ray structures of their complexes with the enzyme.

Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase.,Felder CE, Harel M, Silman I, Sussman JL Acta Crystallogr D Biol Crystallogr. 2002 Oct;58(Pt 10 Pt 2):1765-71. Epub, 2002 Sep 28. PMID:12351819^[1]

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

References

↑ Felder CE, Harel M, Silman I, Sussman JL. Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase. Acta Crystallogr D Biol Crystallogr. 2002 Oct;58(Pt 10 Pt 2):1765-71. Epub, 2002 Sep 28. PMID:12351819

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/1e3q"

@@ 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]], [[1oce|1oce]], [[2dfp|2dfp]], [[1som|1som]], [[2dx6|2dx6]], [[1vxo|1vxo]], [[1vxr|1vxr]], [[1qti|1qti]], [[1qig|1qig]], [[1qih|1qih]], [[1qii|1qii]], [[1qij|1qij]], [[1qik|1qik]], [[1qim|1qim]], [[1qid|1qid]], [[1qie|1qie]], [[1qif|1qif]], [[1eea|1eea]]</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=1e3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e3q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e3q RCSB], [http://www.ebi.ac.uk/pdbsum/1e3q 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=1e3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e3q OCA], [http://pdbe.org/1e3q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e3q RCSB], [http://www.ebi.ac.uk/pdbsum/1e3q 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 1e3q" 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]]
 *[[Acetylcholinesterase|Acetylcholinesterase]]
 == References ==

1e3q

From Proteopedia

Revision as of 02:09, 11 September 2015

TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH BW284C51

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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