4b7z: Difference between revisions
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{{STRUCTURE_4b7z| PDB=4b7z | SCENE= }} | {{STRUCTURE_4b7z| PDB=4b7z | SCENE= }} | ||
===Mus musculus Acetylcholinesterase in complex with N-(2-Diethylamino-ethyl)-1-(4-methylphenyl)-methanesulfonamide=== | ===Mus musculus Acetylcholinesterase in complex with N-(2-Diethylamino-ethyl)-1-(4-methylphenyl)-methanesulfonamide=== | ||
{{ABSTRACT_PUBMED_23984975}} | |||
==Function== | ==Function== | ||
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==About this Structure== | ==About this Structure== | ||
[[4b7z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B7Z OCA]. | [[4b7z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B7Z OCA]. | ||
==Reference== | |||
<ref group="xtra">PMID:023984975</ref><references group="xtra"/><references/> | |||
[[Category: Acetylcholinesterase]] | [[Category: Acetylcholinesterase]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] |
Revision as of 07:13, 12 September 2013
Mus musculus Acetylcholinesterase in complex with N-(2-Diethylamino-ethyl)-1-(4-methylphenyl)-methanesulfonamideMus musculus Acetylcholinesterase in complex with N-(2-Diethylamino-ethyl)-1-(4-methylphenyl)-methanesulfonamide
Template:ABSTRACT PUBMED 23984975
FunctionFunction
[ACES_MOUSE] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.
About this StructureAbout this Structure
4b7z is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Andersson CD, Forsgren N, Akfur C, Allgardsson A, Berg L, Engdahl C, Qian W, Ekstrom FJ, Linusson A. Divergent Structure-Activity Relationships of Structurally Similar Acetylcholinesterase Inhibitors. J Med Chem. 2013 Aug 28. PMID:23984975 doi:10.1021/jm400990p