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==Crystal structure of recombinant human acetylcholinesterase in complex with fasciculin-2==
==Crystal structure of recombinant human acetylcholinesterase in complex with fasciculin-2==
<StructureSection load='4ey8' size='340' side='right' caption='[[4ey8]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='4ey8' size='340' side='right'caption='[[4ey8]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ey8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EY8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EY8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ey8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EY8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACHE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ey8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ey8 OCA], [https://pdbe.org/4ey8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ey8 RCSB], [https://www.ebi.ac.uk/pdbsum/4ey8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ey8 ProSAT]</span></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=4ey8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ey8 OCA], [http://pdbe.org/4ey8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ey8 RCSB], [http://www.ebi.ac.uk/pdbsum/4ey8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ey8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ACES_HUMAN ACES_HUMAN]] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.<ref>PMID:2714437</ref> <ref>PMID:1748670</ref> <ref>PMID:1517212</ref> <ref>PMID:11985878</ref> [[http://www.uniprot.org/uniprot/TXFA2_DENAN TXFA2_DENAN]] This three-finger toxin selectively binds and inhibits with a 1:1 stoichiometry the mammalian and electric fish acetylcholinesterase (AChE) at picomolar concentrations. It is highly specific for the peripheral site on acetylcholinesterase. It has been called fasciculin since after injection into mice it cause severe, generalized and long-lasting (5-7 hours) fasciculations. The whole venom has anticoagulant activity, and the various components seem to act synergistically.
[https://www.uniprot.org/uniprot/ACES_HUMAN ACES_HUMAN] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.<ref>PMID:2714437</ref> <ref>PMID:1748670</ref> <ref>PMID:1517212</ref> <ref>PMID:11985878</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 23: Line 21:
==See Also==
==See Also==
*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
*[[3D structures of acetylcholinesterase|3D structures of acetylcholinesterase]]
*[[Fasciculin|Fasciculin]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acetylcholinesterase]]
[[Category: Dendroaspis angusticeps]]
[[Category: Dendroaspis angusticeps]]
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Burshteyn, F]]
[[Category: Large Structures]]
[[Category: Cassidy, M]]
[[Category: Burshteyn F]]
[[Category: Cheung, J]]
[[Category: Cassidy M]]
[[Category: Franklin, M]]
[[Category: Cheung J]]
[[Category: Gary, E]]
[[Category: Franklin M]]
[[Category: Height, J]]
[[Category: Gary E]]
[[Category: Love, J]]
[[Category: Height J]]
[[Category: Rudolph, M]]
[[Category: Love J]]
[[Category: Fasciculin 2]]
[[Category: Rudolph M]]
[[Category: Hydrolase]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Inhibitor]]
[[Category: Snake venom toxin]]

Revision as of 07:22, 7 October 2022

Crystal structure of recombinant human acetylcholinesterase in complex with fasciculin-2Crystal structure of recombinant human acetylcholinesterase in complex with fasciculin-2

Structural highlights

4ey8 is a 2 chain structure with sequence from Dendroaspis angusticeps and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACES_HUMAN Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.[1] [2] [3] [4]

Publication Abstract from PubMed

Human acetylcholinesterase (AChE) is a significant target for therapeutic drugs. Here we present high resolution crystal structures of human AChE, alone and in complexes with drug ligands; donepezil, an Alzheimer's disease drug, binds differently to human AChE than it does to Torpedo AChE. These crystals of human AChE provide a more accurate platform for further drug development than previously available.

Structures of human acetylcholinesterase in complex with pharmacologically important ligands.,Cheung J, Rudolph MJ, Burshteyn F, Cassidy MS, Gary EN, Love J, Franklin MC, Height JJ J Med Chem. 2012 Oct 4. PMID:23035744[5]

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

See Also

References

  1. ↑ Chhajlani V, Derr D, Earles B, Schmell E, August T. Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase. FEBS Lett. 1989 Apr 24;247(2):279-82. PMID:2714437
  2. ↑ Velan B, Grosfeld H, Kronman C, Leitner M, Gozes Y, Lazar A, Flashner Y, Marcus D, Cohen S, Shafferman A. The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580----Ala mutant. J Biol Chem. 1991 Dec 15;266(35):23977-84. PMID:1748670
  3. ↑ Shafferman A, Kronman C, Flashner Y, Leitner M, Grosfeld H, Ordentlich A, Gozes Y, Cohen S, Ariel N, Barak D, et al.. Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding. J Biol Chem. 1992 Sep 5;267(25):17640-8. PMID:1517212
  4. ↑ Yang L, He HY, Zhang XJ. Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells. Neurosci Res. 2002 Apr;42(4):261-8. PMID:11985878
  5. ↑ Cheung J, Rudolph MJ, Burshteyn F, Cassidy MS, Gary EN, Love J, Franklin MC, Height JJ. Structures of human acetylcholinesterase in complex with pharmacologically important ligands. J Med Chem. 2012 Oct 4. PMID:23035744 doi:http://dx.doi.org/10.1021/jm300871x

4ey8, resolution 2.60Å

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