Slow conformational dynamics of the guanine nucleotide-binding protein Ras complexed with the GTP analogue GTPgammaS.

@article{Spoerner2007SlowCD,
  title={Slow conformational dynamics of the guanine nucleotide-binding protein Ras complexed with the GTP analogue GTPgammaS.},
  author={Michael Spoerner and Andrea Nuehs and Christian Herrmann and Guido Steiner and Hans Robert Kalbitzer},
  journal={The FEBS journal},
  year={2007},
  volume={274 6},
  pages={1419-33}
}
The guanine nucleotide-binding protein Ras occurs in solution in two different conformational states, state 1 and state 2 with an equilibrium constant K(12) of 2.0, when the GTP analogue guanosine-5'-(beta,gamma-imido)triphosphate or guanosine-5'-(beta,gamma-methyleno)triphosphate is bound to the active centre. State 2 is assumed to represent a strong binding state for effectors with a conformation similar to that found for Ras complexed to effectors. In the other state (state 1), the switch… CONTINUE READING

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