2ace
From Proteopedia
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===NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO CALIFORNICA=== | ===NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO CALIFORNICA=== | ||
{{ABSTRACT_PUBMED_8989325}} | {{ABSTRACT_PUBMED_8989325}} | ||
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| + | ==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:008989325</ref><ref group="xtra">PMID:009692976</ref><ref group="xtra">PMID:012505979</ref><references group="xtra"/> | + | <ref group="xtra">PMID:008989325</ref><ref group="xtra">PMID:009692976</ref><ref group="xtra">PMID:012505979</ref><references group="xtra"/><references/> |
[[Category: Acetylcholinesterase]] | [[Category: Acetylcholinesterase]] | ||
[[Category: Torpedo californica]] | [[Category: Torpedo californica]] | ||
Revision as of 12:25, 31 March 2013
Contents |
NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO CALIFORNICA
(-)-Huperzine A (HupA) is found in an extract from a club moss that has been used for centuries in Chinese folk medicine. Its action has been attributed to its ability to strongly inhibit acetylcholinesterase (AChE). The crystal structure of the complex of AChE with optically pure HupA at 2.5 A resolution shows an unexpected orientation for the inhibitor with surprisingly few strong direct interactions with protein residues to explain its high affinity. This structure is compared to the native structure of AChE devoid of any inhibitor as determined to the same resolution. An analysis of the affinities of structural analogues of HupA, correlated with their interactions with the protein, shows the importance of individual hydrophobic interactions between HupA and aromatic residues in the active-site gorge of AChE.
Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A., Raves ML, Harel M, Pang YP, Silman I, Kozikowski AP, Sussman JL, Nat Struct Biol. 1997 Jan;4(1):57-63. PMID:8989325
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
2ace is a 1 chain structure with sequence from Torpedo californica. This structure supersedes the now removed PDB entry 1ace. Full crystallographic information is available from OCA.
See Also
- AChE bivalent inhibitors
- AChE inhibitors and substrates
- AChE inhibitors and substrates (Part III)
- Acetylcholine
- Acetylcholinesterase
- Acetylcholinesterase complexed with N-9-(1'%2C2'%2C3'%2C4'-tetrahydroacridinyl)-1%2C8-diaminooctane
- Acetylcholinesterase with DFP
- Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (5 carbon linker)
- Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (7 carbon linker)
Reference
- Raves ML, Harel M, Pang YP, Silman I, Kozikowski AP, Sussman JL. Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A. Nat Struct Biol. 1997 Jan;4(1):57-63. PMID:8989325
- Williamson PT, Grobner G, Spooner PJ, Miller KW, Watts A. Probing the agonist binding pocket in the nicotinic acetylcholine receptor: a high-resolution solid-state NMR approach. Biochemistry. 1998 Jul 28;37(30):10854-9. PMID:9692976 doi:10.1021/bi980390q
- Bourne Y, Taylor P, Radic Z, Marchot P. Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. EMBO J. 2003 Jan 2;22(1):1-12. PMID:12505979 doi:http://dx.doi.org/10.1093/emboj/cdg005
