2ace
From Proteopedia
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==See Also== | ==See Also== | ||
| - | *[[ACETYLCHOLINESTERASE COMPLEXED WITH N-9-(1'%2C2'%2C3'%2C4'-TETRAHYDROACRIDINYL)-1%2C8-DIAMINOOCTANE|ACETYLCHOLINESTERASE COMPLEXED WITH N-9-(1'%2C2'%2C3'%2C4'-TETRAHYDROACRIDINYL)-1%2C8-DIAMINOOCTANE]] | ||
*[[AChE bivalent inhibitors|AChE bivalent inhibitors]] | *[[AChE bivalent inhibitors|AChE bivalent inhibitors]] | ||
*[[AChE inhibitors and substrates|AChE inhibitors and substrates]] | *[[AChE inhibitors and substrates|AChE inhibitors and substrates]] | ||
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*[[Acetylcholine|Acetylcholine]] | *[[Acetylcholine|Acetylcholine]] | ||
*[[Acetylcholinesterase|Acetylcholinesterase]] | *[[Acetylcholinesterase|Acetylcholinesterase]] | ||
| + | *[[Acetylcholinesterase complexed with N-9-(1'%2C2'%2C3'%2C4'-tetrahydroacridinyl)-1%2C8-diaminooctane|Acetylcholinesterase complexed with N-9-(1'%2C2'%2C3'%2C4'-tetrahydroacridinyl)-1%2C8-diaminooctane]] | ||
| + | *[[Acetylcholinesterase with DFP|Acetylcholinesterase with DFP]] | ||
| + | *[[Acetylcholinesterase with acetylcholine|Acetylcholinesterase with acetylcholine]] | ||
*[[Acetylcholinesterase: Substrate Traffic and Inhibition|Acetylcholinesterase: Substrate Traffic and Inhibition]] | *[[Acetylcholinesterase: Substrate Traffic and Inhibition|Acetylcholinesterase: Substrate Traffic and Inhibition]] | ||
*[[Alzheimer's Disease|Alzheimer's Disease]] | *[[Alzheimer's Disease|Alzheimer's Disease]] | ||
*[[Group:SMART:Acetylcholinesterase:A Story of Substrate Traffic and Inhibition by Green Mamba Snake Toxin|SMART:Acetylcholinesterase:A Story of Substrate Traffic and Inhibition by Green Mamba Snake Toxin]] | *[[Group:SMART:Acetylcholinesterase:A Story of Substrate Traffic and Inhibition by Green Mamba Snake Toxin|SMART:Acetylcholinesterase:A Story of Substrate Traffic and Inhibition by Green Mamba Snake Toxin]] | ||
*[[Structure Gallery Generator|Structure Gallery Generator]] | *[[Structure Gallery Generator|Structure Gallery Generator]] | ||
| + | *[[Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (5 carbon linker)|Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (5 carbon linker)]] | ||
| + | *[[Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (7 carbon linker)|Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (7 carbon linker)]] | ||
*[[User:Wayne Decatur/Biochem642 Molecular Visualization 2010 Fall Sessions|User:Wayne Decatur/Biochem642 Molecular Visualization 2010 Fall Sessions]] | *[[User:Wayne Decatur/Biochem642 Molecular Visualization 2010 Fall Sessions|User:Wayne Decatur/Biochem642 Molecular Visualization 2010 Fall Sessions]] | ||
*[[User:Wayne Decatur/Biochem642 Molecular Visualization Sessions|User:Wayne Decatur/Biochem642 Molecular Visualization Sessions]] | *[[User:Wayne Decatur/Biochem642 Molecular Visualization Sessions|User:Wayne Decatur/Biochem642 Molecular Visualization Sessions]] | ||
Revision as of 07:18, 13 June 2012
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.
About this Structure
2ace is a 1 chain structure of Acetylcholinesterase 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
- Acetylcholinesterase with acetylcholine
- Acetylcholinesterase: Substrate Traffic and Inhibition
- Alzheimer's Disease
- SMART:Acetylcholinesterase:A Story of Substrate Traffic and Inhibition by Green Mamba Snake Toxin
- Structure Gallery Generator
- Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (5 carbon linker)
- Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (7 carbon linker)
- User:Wayne Decatur/Biochem642 Molecular Visualization 2010 Fall Sessions
- User:Wayne Decatur/Biochem642 Molecular Visualization Sessions
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
