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High-frequency 94 GHz ENDOR characterization of the metal binding site in wild type Ras. GDP and its oncogenic mutant G12V in frozen solution

Bennati, M. ; Hertel, M. ; Fritscher, J. ; Prisner, T. ; Weiden, N. ; Hofweber, R. ; Spörner, M. ; Horn, G. ; Kalbitzer, Hans-Robert
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Date of publication of this fulltext: 05 Aug 2009 13:34


Abstract

The guanine nucleotide binding protein Ras plays a central role as molecular switch in cellular signal transduction. Ras cycles between a GDP-bound "off" state and a GTP-bound "on" state. Specific oncogenic mutations in the Ras protein are found in up to 30% of all human tumors. Previous 31P NMR studies had demonstrated that in liquid solution different conformational states in the GDP-bound as ...

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