The Nucleotide Exchange Factor Ric-8 A is a Chaperone for the Conformationally Dynamic Nucleotide-Free State of G Alpha I 1

@inproceedings{Thomas2017TheNE,
  title={The Nucleotide Exchange Factor Ric-8 A is a Chaperone for the Conformationally Dynamic Nucleotide-Free State of G Alpha I 1},
  author={Celestine J. Thomas and Kl{\'a}ra Briknarov{\'a} and Jonathan K. Hilmer and Navid Movahed and Brian Bothner and John P. Sumida and Gregory G Tall and Stephen R Sprang},
  year={2017}
}
Heterotrimeric G protein a subunits are activated upon exchange of GDP for GTP at the nucleotide binding site of Ga, catalyzed by guanine nucleotide exchange factors (GEFs). In addition to transmembrane G protein-coupled receptors (GPCRs), which act on G protein heterotrimers, members of the family cytosolic proteins typified by mammalian Ric-8A are GEFs for Gi/q/12/13-class Ga subunits. Ric-8A binds to GaNGDP, resulting in the release of GDP. The Ric-8A complex with nucleotide-free Gai1 is… CONTINUE READING

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