7e3d: Difference between revisions

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'''Unreleased structure'''


The entry 7e3d is ON HOLD  until Paper Publication
==Crystal structure of human acetylcholinesterase==
<StructureSection load='7e3d' size='340' side='right'caption='[[7e3d]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7e3d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E3D FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PE8:3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL'>PE8</scene></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=7e3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e3d OCA], [https://pdbe.org/7e3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e3d RCSB], [https://www.ebi.ac.uk/pdbsum/7e3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e3d ProSAT]</span></td></tr>
</table>
== Function ==
[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>


Authors: Dileep, K.V., Ihara, K., Mishima-Tsumagari, C., Kukimoto-Niino, M., Yonemochi, M., Hanada, K., Shirouzu, M., Zhang, K.Y.J.
==See Also==
 
*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
Description: Crystal structure of human acetylcholinesterase
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Zhang, K.Y.J]]
__TOC__
[[Category: Hanada, K]]
</StructureSection>
[[Category: Shirouzu, M]]
[[Category: Homo sapiens]]
[[Category: Yonemochi, M]]
[[Category: Large Structures]]
[[Category: Mishima-Tsumagari, C]]
[[Category: Dileep KV]]
[[Category: Dileep, K.V]]
[[Category: Hanada K]]
[[Category: Kukimoto-Niino, M]]
[[Category: Ihara K]]
[[Category: Ihara, K]]
[[Category: Kukimoto-Niino M]]
[[Category: Mishima-Tsumagari C]]
[[Category: Shirouzu M]]
[[Category: Yonemochi M]]
[[Category: Zhang KYJ]]

Latest revision as of 19:45, 29 November 2023

Crystal structure of human acetylcholinesteraseCrystal structure of human acetylcholinesterase

Structural highlights

7e3d is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
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]

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

7e3d, resolution 2.50Å

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