Binding of Rac1, Rnd1, and RhoD to a novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain.

@article{Tong2007BindingOR,
  title={Binding of Rac1, Rnd1, and RhoD to a novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain.},
  author={Yufeng Tong and Preeti Chugha and Prasanta K. Hota and Rebecca S Alviani and Mei Li and Wolfram Tempel and Limin Shen and Hee-won Park and Matthias Buck},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 51},
  pages={
          37215-24
        }
}
Plexins are the first known transmembrane receptors that interact directly with small GTPases. On binding to certain Rho family GTPases, the receptor regulates the remodeling of the actin cytoskeleton and alters cell movement in response to semaphorin guidance cues. In a joint solution NMR spectroscopy and x-ray crystallographic study, we characterize a 120-residue cytoplasmic independent folding domain of plexin-B1 that directly binds three Rho family GTPases, Rac1, Rnd1, and RhoD. The NMR… CONTINUE READING