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

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⋅M...

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Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2010-05, Vol.49 (22), p.3830-3833
Main Authors: Rosnizeck, Ina C, Graf, Thorsten, Spoerner, Michael, Tränkle, Jens, Filchtinski, Daniel, Herrmann, Christian, Gremer, Lothar, Vetter, Ingrid R, Wittinghofer, Alfred, König, Burkhard, Kalbitzer, Hans Robert
Format: Article
Language:English
Subjects:
Affinity
Binding
Binding Sites
Coordination Complexes - chemistry
Crystallography, X-Ray
cyclen
Drug Design
Effectors
Heterocyclic Compounds - chemistry
Human
Humans
Inhibition
Inhibitors
Magnetic Resonance Spectroscopy
NMR spectroscopy
Pictures
Protein Binding
Protein Stability
Protein Structure, Tertiary
Proteins
Ras protein
ras Proteins - chemistry
signal transduction
Zinc
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Summary: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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200907002