4ey5: Difference between revisions
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{{STRUCTURE_4ey5| PDB=4ey5 | SCENE= }} | {{STRUCTURE_4ey5| PDB=4ey5 | SCENE= }} | ||
===Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with (-)-huperzine A=== | ===Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with (-)-huperzine A=== | ||
{{ABSTRACT_PUBMED_23035744}} | |||
==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> | |||
==About this Structure== | ==About this Structure== | ||
[[4ey5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EY5 OCA]. | [[4ey5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EY5 OCA]. | ||
==See Also== | |||
*[[Acetylcholinesterase|Acetylcholinesterase]] | |||
==Reference== | |||
<ref group="xtra">PMID:023035744</ref><references group="xtra"/><references/> | |||
[[Category: Acetylcholinesterase]] | [[Category: Acetylcholinesterase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 08:09, 23 October 2013
Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with (-)-huperzine ACrystal Structure of Recombinant Human Acetylcholinesterase in Complex with (-)-huperzine A
Template:ABSTRACT PUBMED 23035744
FunctionFunction
[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]
About this StructureAbout this Structure
4ey5 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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