1gpn: Difference between revisions
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STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH HUPERZINE B AT 2.35A RESOLUTION
OverviewOverview
Kinetic and structural data are presented on the interaction with Torpedo, californica acetylcholinesterase (TcAChE) of (+)-huperzine A, a synthetic, enantiomer of the anti-Alzheimer drug, (-)-huperzine A, and of its natural, homologue (-)-huperzine B. (+)-Huperzine A and (-)-huperzine B bind to the, enzyme with dissociation constants of 4.30 and 0.33 microM, respectively, compared to 0.18 microM for (-)-huperzine A. The X-ray structures of the, complexes of (+)-huperzine A and (-)-huperzine B with TcAChE were, determined to 2.1 and 2.35 A resolution, respectively, and compared to the, previously determined structure of the (-)-huperzine A complex. All three, interact with the "anionic" subsite of the active site, primarily through, pi-pi stacking and through van der Waals or C-H.pi ... [(full description)]
About this StructureAbout this Structure
1GPN is a [Single protein] structure of sequence from [Torpedo californica] with NAG and HUB as [ligands]. Active as [Acetylcholinesterase], with EC number [3.1.1.7]. Structure known Active Site: HUB. Full crystallographic information is available from [OCA].
ReferenceReference
X-ray structures of Torpedo californica acetylcholinesterase complexed with (+)-huperzine A and (-)-huperzine B: structural evidence for an active site rearrangement., Dvir H, Jiang HL, Wong DM, Harel M, Chetrit M, He XC, Jin GY, Yu GL, Tang XC, Silman I, Bai DL, Sussman JL, Biochemistry. 2002 Sep 3;41(35):10810-8. PMID:12196020
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