RAS residues that are distant from the GDP binding site play a critical role in dissociation factor-stimulated release of GDP.

@article{Verrotti1992RASRT,
  title={RAS residues that are distant from the GDP binding site play a critical role in dissociation factor-stimulated release of GDP.},
  author={A C Verrotti and J B Cr{\'e}chet and Francesco Di Blasi and Gregorio Seidita and Mario G. Mirisola and C A Kavounis and Vassilios Nastopoulos and E Burderi and Emmanuele De Vendittis and Andrea Parmeggiani},
  journal={The EMBO journal},
  year={1992},
  volume={11 8},
  pages={2855-62}
}
We have previously shown that a conserved glycine at position 82 of the yeast RAS2 protein is involved in the conversion of RAS proteins from the GDP- to the GTP-bound form. We have now investigated the role of glycine 82 and neighbouring amino acids of the distal switch II region in the physiological mechanism of activation of RAS. We have introduced single and double amino acid substitutions at positions 80-83 of the RAS2 gene, and we have investigated the interaction of the corresponding… CONTINUE READING