Effector recognition by the small GTP-binding proteins Ras and Ral.

@article{Bauer1999EffectorRB,
  title={Effector recognition by the small GTP-binding proteins Ras and Ral.},
  author={Bianca Bauer and Gladys Mirey and Ingrid R. Vetter and Juan Antonio Garcia-Ranea and Alfonso Valencia and Alfred Wittinghofer and Jacques H. Camonis and Robbert H. Cool},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 25},
  pages={17763-70}
}
The Ral effector protein RLIP76 (also called RIP/RalBP1) binds to Ral.GTP via a region that shares no sequence homology with the Ras-binding domains of the Ser/Thr kinase c-Raf-1 and the Ral-specific guanine nucleotide exchange factors. Whereas the Ras-binding domains have a similar ubiquitin-like structure, the Ral-binding domain of RLIP was predicted to comprise a coiled-coil region. In order to obtain more information about the specificity and the structural mode of the interaction between… CONTINUE READING

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