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

Rosnizeck Ina C. | Zendy; Graf Thorsten | Zendy; Spoerner Michael | Zendy; Tränkle Jens | Zendy; Filchtinski Daniel | Zendy; Herrmann Christian | Zendy; Gremer Lothar | Zendy; Vetter Ingrid R. | Zendy; Wittinghofer Alfred | Zendy; König Burkhard | Zendy; Kalbitzer Hans Robert | Zendy

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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.

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