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The Tubulin-Bound Structure of the Antimitotic Drug Tubulysin

Authors

  • Karel Kubicek Dr.,

    1. Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen (Germany)
    2. Present address: Department of Condensed Matter Physics, Faculty of Science, Brno (Czech Republic)
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    • These authors contributed equally to this work.

  • S. Kaspar Grimm Dr.,

    1. Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen (Germany)
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    • These authors contributed equally to this work.

  • Julien Orts Dr.,

    1. EMBL, Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg (Germany)
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  • Florenz Sasse Dr.,

    1. Department of Chemical Biology and Medicinal Chemistry at the Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstrasse 7, 38124 Braunschweig (Germany)
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  • Teresa Carlomagno Priv.-Doz. Dr.

    1. EMBL, Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg (Germany)
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Abstract

original image

Bound to be active: The solution structure of tubulin-bound tubulysin A is determined from transferred NOE data (see picture; blue N, red O, yellow S, green C), and this bioactive conformation is compared to the unbound conformation. The binding site on tubulin is examined on the basis of the interligand NOEs observed between epothilone A and tubulysin A in the presence of tubulin.

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