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Stabilizing a Weak Binding State for Effectors in the Human Ras Protein by Cyclen Complexes
Author(s) -
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
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200907002
Subject(s) - cyclen , effector , chemistry , stereochemistry , binding site , computational biology , biochemistry , biophysics , crystallography , biology
En route to new inhibitors : The binding of Zn 2+ 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⋅Mg 2+ ⋅GppNHp complexed to Zn 2+ cyclen.