Stabilizing a Weak Binding State for Effectors in the Human Ras Protein by Cyclen Complexes

作者：Ina C. Rosnizeck, Thorsten Gräf, Michael Spoerner, Jens Tränkle, Daniel Filchtinski, Christian Herrmann, Lothar Gremer, Ingrid R. Vetter, Alfred Wittinghofer, Burkhard König, Hans Robert Kalbitzer · 发表于：Angewandte Chemie International Edition · 年份：2010 · DOI：10.1002/anie.200907002 · 被引用次数：108 · 研究领域：Protein Kinase Regulation and GTPase Signaling、Ion channel regulation and function、Synthesis and Reactivity of Heterocycles

En route to new inhibitors: The binding of Zn2+ cyclen to the human Ras protein stabilizes a protein conformation that has a weak affinity for effectors. Consequently this complex is a lead structure for inhibition studies on the Ras–effector interaction. The picture shows the NMR structure of Ras⋅Mg2+⋅GppNHp complexed to Zn2+ cyclen.