1h23: Difference between revisions

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{{STRUCTURE_1h23|  PDB=1h23  |  SCENE=  }}  
{{STRUCTURE_1h23|  PDB=1h23  |  SCENE=  }}  
===STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH (S,S)-(-)-BIS(12)-HUPYRIDONE AT 2.15A RESOLUTION===
===Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with (S,S)-(-)-bis(12)-hupyridone at 2.15A resolution===
{{ABSTRACT_PUBMED_12517147}}
{{ABSTRACT_PUBMED_12517147}}
==Function==
[[http://www.uniprot.org/uniprot/ACES_TORCA 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.


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:012517147</ref><ref group="xtra">PMID:010934357</ref><references group="xtra"/>
<ref group="xtra">PMID:012517147</ref><references group="xtra"/><references/>
[[Category: Acetylcholinesterase]]
[[Category: Acetylcholinesterase]]
[[Category: Torpedo californica]]
[[Category: Torpedo californica]]

Revision as of 05:45, 22 January 2014

Template:STRUCTURE 1h23

Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with (S,S)-(-)-bis(12)-hupyridone at 2.15A resolution

Template:ABSTRACT PUBMED 12517147

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.

About this Structure

1h23 is a 1 chain structure with sequence from Torpedo californica. Full crystallographic information is available from OCA.

See Also

Reference

  1. Wong DM, Greenblatt HM, Dvir H, Carlier PR, Han YF, Pang YP, Silman I, Sussman JL. Acetylcholinesterase complexed with bivalent ligands related to huperzine a: experimental evidence for species-dependent protein-ligand complementarity. J Am Chem Soc. 2003 Jan 15;125(2):363-73. PMID:12517147 doi:https://dx.doi.org/10.1021/ja021111w

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