1h22
From Proteopedia
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{{STRUCTURE_1h22| PDB=1h22 | SCENE= }} | {{STRUCTURE_1h22| PDB=1h22 | SCENE= }} | ||
===STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH (S,S)-(-)-BIS(10)-HUPYRIDONE AT 2.15A RESOLUTION=== | ===STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH (S,S)-(-)-BIS(10)-HUPYRIDONE AT 2.15A RESOLUTION=== | ||
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*[[AChE bivalent inhibitors|AChE bivalent inhibitors]] | *[[AChE bivalent inhibitors|AChE bivalent inhibitors]] | ||
*[[Acetylcholinesterase|Acetylcholinesterase]] | *[[Acetylcholinesterase|Acetylcholinesterase]] | ||
- | *[[Alzheimer's Disease|Alzheimer's Disease]] | ||
*[[Torpedo Californica Acetylcholinesterase in complex with an (R)-Tacrine-(10)-Hupyridone inhibitor|Torpedo Californica Acetylcholinesterase in complex with an (R)-Tacrine-(10)-Hupyridone inhibitor]] | *[[Torpedo Californica Acetylcholinesterase in complex with an (R)-Tacrine-(10)-Hupyridone inhibitor|Torpedo Californica Acetylcholinesterase in complex with an (R)-Tacrine-(10)-Hupyridone inhibitor]] | ||
*[[User:Dawn M. Wong|User:Dawn M. Wong]] | *[[User:Dawn M. Wong|User:Dawn M. Wong]] |
Revision as of 12:35, 26 July 2012
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
About this Structure
1h22 is a 1 chain structure of Acetylcholinesterase with sequence from Torpedo californica. Full crystallographic information is available from OCA.
See Also
- AChE bivalent inhibitors
- Acetylcholinesterase
- Torpedo Californica Acetylcholinesterase in complex with an (R)-Tacrine-(10)-Hupyridone inhibitor
- User:Dawn M. Wong
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
- Carlier PR, Du DM, Han YF, Liu J, Perola E, Williams ID, Pang YP. Dimerization of an Inactive Fragment of Huperzine A Produces a Drug with Twice the Potency of the Natural Product This work was supported by the Research Grants Council of Hong Kong (HKUST6156/97M), the Biotechnology Research Institute (HKUST), the Mayo Foundation, and the Istituto Pasteur Fondazione Cenci Bolognetti (E.P.). We thank Prof. X. C. Tang (Shanghai Institute of Materia Medica) for a gift of (-)-1. Angew Chem Int Ed Engl. 2000 May 15;39(10):1775-1777. PMID:10934357
- 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
- Pang YP, Kozikowski AP. Prediction of the binding sites of huperzine A in acetylcholinesterase by docking studies. J Comput Aided Mol Des. 1994 Dec;8(6):669-81. PMID:7738603
- Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science. 1991 Aug 23;253(5022):872-9. PMID:1678899
Categories: Acetylcholinesterase | Torpedo californica | Carlier, P R. | Greenblatt, H M. | Han, Y F. | Pang, Y P. | Silman, I. | Sussman, J L. | Wong, D M. | Alzheimer's disease | Bivalent ligand | Dual-site binding | Glycoprotein | Gpi-anchor neurotransmitter degradation | Huperzine some | Hydrolase | Inhibitor | Membrane | Muscle | Nerve | Neurotransmitter cleavage | Serine esterase synapse | Serine hydrolase