Title : Influence of guanine nucleotides on complex formation between Ras and CDC25 proteins.

Pub. Date : 1993 Mar

PMID : 8441380






4 Functional Relationships(s)
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1 The CDC25 fusion protein catalyzed replacement of GDP-bound to Ras2 with GTP (activation) more efficiently than that of the reverse reaction of replacement of GTP for GDP (deactivation), consistent with prior genetic analysis of CDC25 which indicated a positive role in the activation of Ras. Guanosine Diphosphate Ras family guanine nucleotide exchange factor CDC25 Saccharomyces cerevisiae S288C
2 The CDC25 fusion protein catalyzed replacement of GDP-bound to Ras2 with GTP (activation) more efficiently than that of the reverse reaction of replacement of GTP for GDP (deactivation), consistent with prior genetic analysis of CDC25 which indicated a positive role in the activation of Ras. Guanosine Diphosphate Ras family guanine nucleotide exchange factor CDC25 Saccharomyces cerevisiae S288C
3 This higher affinity of CDC25 for the nucleotide-free form than for either the GDP- or GTP-bound form suggests that CDC25 catalyzes exchange of guanine nucleotides bound to Ras proteins by stabilization of the transitory nucleotide-free state. Guanosine Diphosphate Ras family guanine nucleotide exchange factor CDC25 Saccharomyces cerevisiae S288C
4 This higher affinity of CDC25 for the nucleotide-free form than for either the GDP- or GTP-bound form suggests that CDC25 catalyzes exchange of guanine nucleotides bound to Ras proteins by stabilization of the transitory nucleotide-free state. Guanosine Diphosphate Ras family guanine nucleotide exchange factor CDC25 Saccharomyces cerevisiae S288C