Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily.

@article{Linnemann1999ThermodynamicAK,
  title={Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily.},
  author={Thomas Linnemann and Matthias Geyer and B K Jaitner and Christoph Block and Hans Robert Kalbitzer and Alfred Wittinghofer and Christian Herrmann},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 19},
  pages={13556-62}
}
Cellular signaling downstream of Ras is highly diversified and may involve many different effector molecules. A potential candidate is AF6 which was originally identified as a fusion to ALL-1 in acute myeloid leukemia. In the present work the interaction between Ras and AF6 is characterized and compared with other effectors. The binding characteristics are quite similar to Raf and RalGEF, i.e. nucleotide dissociation as well as GTPase-activating protein activity are inhibited, whereas the… CONTINUE READING

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