Conformational States of Human Rat Sarcoma (Ras) Protein Complexed with Its Natural Ligand GTP and Their Role for Effector Interaction and GTP Hydrolysis*

@article{Spoerner2010ConformationalSO,
  title={Conformational States of Human Rat Sarcoma (Ras) Protein Complexed with Its Natural Ligand GTP and Their Role for Effector Interaction and GTP Hydrolysis*},
  author={M. Spoerner and Constantin Hozsa and Johann A. Poetzl and K. Reiss and P. Ganser and M. Geyer and H. Kalbitzer},
  journal={The Journal of Biological Chemistry},
  year={2010},
  volume={285},
  pages={39768 - 39778}
}
The guanine nucleotide-binding protein Ras exists in solution in two different conformational states when complexed with different GTP analogs such as GppNHp or GppCH2p. State 1 has only a very low affinity to effectors and seems to be recognized by guanine nucleotide exchange factors, whereas state 2 represents the high affinity effector binding state. In this work we investigate Ras in complex with the physiological nucleoside triphosphate GTP. By polarization transfer 31P NMR experiments and… Expand
State 1(T) inhibitors of activated Ras.
Cu2+-cyclen as probe to identify conformational states in guanine nucleotide binding proteins.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 44 REFERENCES
Structural Basis for Conformational Dynamics of GTP-bound Ras Protein*
Crystal Structure of M-Ras Reveals a GTP-bound “Off” State Conformation of Ras Family Small GTPases*
...
1
2
3
4
5
...