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Modelling of Biomolecular Structures and Mechanisms pp 11–23Cite as

Binding Sites of Acetylcholine in the Aromatic Gorge Leading to the Active Site of Acetylcholinesterase

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Part of the book series: The Jerusalem Symposia on Quantum Chemistry and Biochemistry ((JSQC,volume 27))

Abstract

Theoretical calculations performed on the interactions of acetylcholine with the ‘aromatic gorge’ of acetylcholinesterase indicate the existence of a number of local minima for the substrate. These minima are clustered in four regions of increasing interactions from top to bottom of the gorge, culminating in the region of the ‘active site’. The results allow the delineation of the role of the different aminoacids lining the walls, emphasizing, in particular, that of Trp 279 and Trp 84 while smaller interactions involve tyrosines 70, 121, 130, 334 and Phe 330. The influence of D72 is stressed, as well as the orientating role of A 201 and the strong driving influence of E199.

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Authors and Affiliations

  1. Institut de Biologie Physico-Chimique, Fondation Edmond de Rothschild, 13, rue Pierre et Marie Curie, 75005, Paris, France

    Alberte Pullman

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  1. Alberte Pullman
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Editors and Affiliations

  1. Fondation Edmond de Rothschild, Institut de Biologie Physico-Chimique, Paris, France

    A. Pullman  & B. Pullman  & 

  2. The Israel Academy of Sciences and Humanities, Jerusalem, Israel

    J. Jortner

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© 1995 Springer Science+Business Media Dordrecht

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Pullman, A. (1995). Binding Sites of Acetylcholine in the Aromatic Gorge Leading to the Active Site of Acetylcholinesterase. In: Pullman, A., Jortner, J., Pullman, B. (eds) Modelling of Biomolecular Structures and Mechanisms. The Jerusalem Symposia on Quantum Chemistry and Biochemistry, vol 27. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-0497-5_2

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  • DOI: https://doi.org/10.1007/978-94-011-0497-5_2

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-4222-2

  • Online ISBN: 978-94-011-0497-5

  • eBook Packages: Springer Book Archive

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