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1vot
From Proteopedia
| 1vot, resolution 2.50Å () | |||||
|---|---|---|---|---|---|
| Sites: | |||||
| Ligands: | |||||
| Activity: | Acetylcholinesterase, with EC number 3.1.1.7 | ||||
| Domains: | Esterase_lipase, COesterase | ||||
| |||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||
| Coordinates: | save as pdb, mmCIF, xml | ||||
ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH HUPERZINE A
Overview
(-)-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 Å 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 gorge of AChE.
About this Structure
1VOT is a Single protein structure of sequence from Torpedo californica. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 00:26:42 2008
