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1h22

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{{STRUCTURE_1h22| PDB=1h22 | SCENE= }}
{{STRUCTURE_1h22| PDB=1h22 | SCENE= }}
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===STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH (S,S)-(-)-BIS(10)-HUPYRIDONE AT 2.15A RESOLUTION===
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===Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with (S,S)-(-)-bis(10)-hupyridone at 2.15A resolution===
{{ABSTRACT_PUBMED_12517147}}
{{ABSTRACT_PUBMED_12517147}}
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==Function==
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[[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==
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<ref group="xtra">PMID:012517147</ref><ref group="xtra">PMID:010934357</ref><references group="xtra"/>
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<ref group="xtra">PMID:012517147</ref><references group="xtra"/><references/>
[[Category: Acetylcholinesterase]]
[[Category: Acetylcholinesterase]]
[[Category: Torpedo californica]]
[[Category: Torpedo californica]]

Revision as of 05:59, 22 January 2014

Template:STRUCTURE 1h22

Contents

Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with (S,S)-(-)-bis(10)-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

1h22 is a 1 chain structure with sequence from Torpedo californica. Full crystallographic information is available from OCA.

See Also

Reference

  • 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:http://dx.doi.org/10.1021/ja021111w

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OCA

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