[HTML][HTML] p120 Ras GTPase-activating protein interacts with Ras-GTP through specific conserved residues

W Miao, L Eichelberger, L Baker… - Journal of Biological …, 1996 - ASBMB
Previous structural studies of RasGAP have failed to clearly localize sites of Ras interaction
to individual amino acids. Hypothesizing that sites of interaction with Ras-GTP would be
conserved, 11 of the most highly conserved amino acid residues of RasGAP were changed
by mutation. Each mutant protein was purified as a glutathione S-transferase catalytic
domain fusion and analyzed for protein stability, Ras GTPase stimulating activity, affinity for
Ras-GTP, and when possible, secondary structure. The majority of conserved positions were …