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A common pharmacophore for a diverse set of colchicine site inhibitors using a structure-based approach

  1. Author:
    Nguyen, T. L.
    McGrath, C.
    Hermone, A. R.
    Burnett, J. C.
    Zaharevitz, D. W.
    Day, B. W.
    Wipf, P.
    Hamel, E.
    Gussio, R.
  2. Author Address

    NCI, Dev Therapeut Program, Target Struct Based Drug Discovery Grp, Frederick, MD 21702 USA. Univ Pittsburgh, Dept Pharmaceut Sci, Pittsburgh, PA 15261 USA. Univ Pittsburgh, Dept Chem, Pittsburgh, PA 15260 USA. Univ Pittsburgh, Ctr Chem Methodol & Lib Dev, Pittsburgh, PA 15260 USA. NCI, Div Canc Treatment & Diag, Dev Therapeut Program, Screening Technol Branch, Frederick, MD 21702 USA Nguyen, TL, NCI, Dev Therapeut Program, Target Struct Based Drug Discovery Grp, Frederick, MD 21702 USA
    1. Year: 2005
    2. Date: SEP 22
  1. Journal: Journal of Medicinal Chemistry
    1. 48
    2. 19
    3. Pages: 6107-6116
  2. Type of Article: Article
  1. Abstract:

    Modulating the structure and function of tubulin and microtubules is an important route to anticancer therapeutics, and therefore, small molecules that bind to tubulin and cause mitotic arrest are of immense interest. A large number of synthetic and natural compounds with diverse structures have been shown to bind at the colchicine site, one of the major binding sites on tubulin, and inhibit tubulin assembly. Using the recently determined X-ray structure of the tubulin:colchicinoid complex as the template, we employed docking studies to determine the binding modes of a set of structurally diverse colchicine site inhibitors. These binding models were subsequently used to construct a comprehensive, structure-based pharmacophore that in combination with molecular dynamics simulations confirms and extends our understanding of binding interactions at the colchicine site

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External Sources

  1. WOS: 000232080200022

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