Affinity-Based Labeling of Cytohesins with a Bifunctional SecinH3 Photoaffinity Probe

Authors

  • Xihe Bi Dr.,

    1. LIMES Institute Program Unit Chemical Biology & Medicinal Chemistry, Universität Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn (Germany), Fax: (+49) 228-735-388
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  • Anton Schmitz Dr.,

    1. LIMES Institute Program Unit Chemical Biology & Medicinal Chemistry, Universität Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn (Germany), Fax: (+49) 228-735-388
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  • Alaa M. Hayallah Dr.,

    1. LIMES Institute Program Unit Chemical Biology & Medicinal Chemistry, Universität Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn (Germany), Fax: (+49) 228-735-388
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  • Jin-Na Song Dr.,

    1. LIMES Institute Program Unit Chemical Biology & Medicinal Chemistry, Universität Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn (Germany), Fax: (+49) 228-735-388
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  • Michael Famulok Prof. Dr.

    1. LIMES Institute Program Unit Chemical Biology & Medicinal Chemistry, Universität Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn (Germany), Fax: (+49) 228-735-388
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  • This research was supported by the SFBs 645 and 704 (M.F.) and by the Alexander von Humboldt Foundation (X.B.).

Abstract

original image

The specific binding of the cytohesin inhibitor SecinH3 to Sec7 domains of cytohesins was shown by the use of a bifunctional photoaffinity probe (see structure) on guanine nucleotide exchange factors (GEFs) and GTPases. This probe should be useful for the proteome-wide profiling of cytohesin complexes and the identification of the binding site.

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