Analysis of Ras Structure and Dynamics by Nuclear Magnetic Resonance

  • S. L. Campbell-Burk
  • T. E. Van Aken
Part of the Handbook of Experimental Pharmacology book series (HEP, volume 108 / 1)


ras oncogenes are among the most prevalent found in human tumors (Barbacid 1987; Bos 1989). These genes encode highly related 21 kDa guanine nucleotide binding proteins which are located on the inner surface of the plasma membrane. They are believed to function as signal switch molecules which relay extracellular growth promoting signals to intracellular targets by cycling between the biologically active ras.GTP and the inactive ras.GDP forms. The on (ras.GTP) and off (ras.GDP) states of the ras signal switch are modulated by interactions with intracellular proteins. Factors which stimulate GDP dissociation are believed to promote GTP formation in vivo (Downward et al. 1990; West et al. 1990; Huang et al. 1990). The inactive GDP form is generated via interaction with GTPase activating proteins, GAP and NF1, to promote hydrolysis of GTP to GDP (Trahey and MscCormick 1987; Gibbs et al. 1988; Martin et al. 1990; Xu et al. 1990; Ballester et al. 1990). Ras proteins acquire oncogenic properties if activated by point mutations that affect binding, dissociation and/or hydrolysis of guanine nucleotide to favor the GTP form of the protein.


Nuclear Magnetic Resonance Nuclear Magnetic Resonance Spectroscopy Nuclear Magnetic Resonance Data Amide Proton Nuclear Magnetic Resonance Study 
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© Springer-Verlag Berlin Heidelberg 1993

Authors and Affiliations

  • S. L. Campbell-Burk
  • T. E. Van Aken

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