A catalytic coiled coil: structural insights into the activation of the Rab GTPase Sec4p by Sec2p.

@article{Dong2007ACC,
  title={A catalytic coiled coil: structural insights into the activation of the Rab GTPase Sec4p by Sec2p.},
  author={Gang Dong and Martina Medkova and Peter J. Novick and Karin M Reinisch},
  journal={Molecular cell},
  year={2007},
  volume={25 3},
  pages={455-62}
}
Rab GTPases, the largest subgroup in the superfamily of Ras-like GTPases, play regulatory roles in multiple steps of intracellular vesicle trafficking. They are activated by guanine nucleotide exchange factors (GEFs), which catalyze the interconversion of the GDP-bound, or inactive, form of Rab to the GTP-bound, or active, form. Relatively little is known of the mechanisms by which GEFs activate Rabs. Here, we present the crystal structure of the GEF domain of Sec2p in complex with its Rab… CONTINUE READING
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