Stabilizing a Weak Binding State for Effectors in the Human Ras Protein by Cyclen Complexes (pages 3830–3833)
Ina C. Rosnizeck, Thorsten Graf, Michael Spoerner, Jens Tränkle, Daniel Filchtinski, Christian Herrmann, Lothar Gremer, Ingrid R. Vetter, Alfred Wittinghofer, Burkhard König and Hans Robert Kalbitzer
Article first published online: 16 APR 2010 | DOI: 10.1002/anie.200907002
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.