1h22

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Template:STRUCTURE 1h22

Contents 1 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH (S,S)-(-)-BIS(10)-HUPYRIDONE AT 2.15A RESOLUTION 2 About this Structure 3 See Also 4 Reference

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 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