Structural determinants for GoLoco-induced inhibition of nucleotide release by Gα subunits

@article{Kimple2002StructuralDF,
  title={Structural determinants for GoLoco-induced inhibition of nucleotide release by G$\alpha$ subunits},
  author={Randall J. Kimple and Michelle E. Kimple and Laurie Betts and John Sondek and D. Siderovski},
  journal={Nature},
  year={2002},
  volume={416},
  pages={878-881}
}
Heterotrimeric G-proteins bind to cell-surface receptors and are integral in transmission of signals from outside the cell. Upon activation of the Gα subunit by binding of GTP, the Gα and Gβγ subunits dissociate and interact with effector proteins for signal transduction. Regulatory proteins with the 19-amino-acid GoLoco motif can bind to Gα subunits and maintain G-protein subunit dissociation in the absence of Gα activation. Here we describe the structural determinants of GoLoco activity as… 

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